3.6: Nucleic Acids - Biology

3.6: Nucleic Acids - Biology

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What you’ll learn to do: Discuss nucleic acids and the role they play in DNA and RNA

Humans have two types of nucleic acids in their bodies: DNA and RNA. But what makes up our DNA?

In this outcome, we’ll learn about the components of DNA and RNA and get a brief introduction to how they work.

Learning Objectives

  • Describe the basic structure of nucleic acids
  • Compare and contrast the structure of DNA and RNA

Structure of Nucleic Acids

Nucleic acids are key macromolecules in the continuity of life. They carry the genetic blueprint of a cell and carry instructions for the functioning of the cell.

The two main types of nucleic acids are deoxyribonucleic acid (DNA) and ribonucleic acid (RNA). DNA is the genetic material found in all living organisms, ranging from single-celled bacteria to multicellular mammals.

The other type of nucleic acid, RNA, is mostly involved in protein synthesis. The DNA molecules never leave the nucleus, but instead use an RNA intermediary to communicate with the rest of the cell. Other types of RNA are also involved in protein synthesis and its regulation.

DNA and RNA are made up of monomers known as nucleotides. The nucleotides combine with each other to form a polynucleotide, DNA or RNA. Each nucleotide is made up of three components: a nitrogenous base, a pentose (five-carbon) sugar, and a phosphate group (Figure 2). Each nitrogenous base in a nucleotide is attached to a sugar molecule, which is attached to a phosphate group. The nucleotides link together by phosphodiester bonds to form the polynucleotide.

DNA Double-Helical Structure

DNA has a double-helical structure (Figure 3). It is composed of two strands, or polymers, of nucleotides. The strands are formed with covalent bonds between phosphate and sugar groups of adjacent nucleotides.

The two strands are bonded to each other at their bases with hydrogen bonds, and the strands coil about each other along their length, hence the “double helix” description, which means a double spiral.

The alternating sugar and phosphate groups lie on the outside of each strand, forming the backbone of the DNA. The nitrogenous bases are stacked in the interior, like the steps of a staircase, and these bases pair; the pairs are bound to each other by hydrogen bonds. The bases pair in such a way that the distance between the backbones of the two strands is the same all along the molecule.


While DNA and RNA are similar, they have very distinct differences. Table 1 summarizes features of DNA and RNA.

Table 1. Features of DNA and RNA
FunctionCarries genetic informationInvolved in protein synthesis
LocationRemains in the nucleusLeaves the nucleus
StructureDNA is double-stranded “ladder”: sugar-phosphate backbone, with base rungs.Usually single-stranded
PyrimidinesCytosine, thymineCytosine, uracil
PurinesAdenine, guanineAdenine, guanine

One other difference bears mention. There is only one type of DNA. DNA is the heritable information that is passed along to each generation of cells; its strands can be “unzipped” with small amount of energy when DNA needs to replicate, and DNA is transcribed into RNA. There are mutliple types of RNA: Messenger RNA is a temporary molecule that transports the information necessary to make a protein from the nucleus (where the DNA remains) to the cytoplasm, where the ribosomes are. Other kinds of RNA include ribosomal RNA (rRNA), transfer RNA (tRNA), small nuclear RNA (snRNA), and microRNA.

Even though the RNA is single stranded, most RNA types show extensive intramolecular base pairing between complementary sequences, creating a predictable three-dimensional structure essential for their function.

As you will learn later, information flow in an organism takes place from DNA to RNA to protein. DNA dictates the structure of mRNA in a process known as transcription, and RNA dictates the structure of protein in a process known as translation. This is known as the Central Dogma of Life, which holds true for all organisms; however, exceptions to the rule occur in connection with viral infections.

Learning Objectives

Nucleic acids are molecules made up of nucleotides that direct cellular activities such as cell division and protein synthesis. Each nucleotide is made up of a pentose sugar, a nitrogenous base, and a phosphate group. There are two types of nucleic acids: DNA and RNA. DNA carries the genetic blueprint of the cell and is passed on from parents to offspring (in the form of chromosomes). It has a double-helical structure with the two strands running in opposite directions, connected by hydrogen bonds, and complementary to each other. RNA is single-stranded and is made of a pentose sugar (ribose), a nitrogenous base, and a phosphate group. RNA is involved in protein synthesis and its regulation. Messenger RNA (mRNA) is copied from the DNA, is exported from the nucleus to the cytoplasm, and contains information for the construction of proteins. Ribosomal RNA (rRNA) is a part of the ribosomes at the site of protein synthesis, whereas transfer RNA (tRNA) carries the amino acid to the site of protein synthesis. microRNA regulates the use of mRNA for protein synthesis.

Check Your Understanding

Answer the question(s) below to see how well you understand the topics covered in the previous section. This short quiz does not count toward your grade in the class, and you can retake it an unlimited number of times.

Use this quiz to check your understanding and decide whether to (1) study the previous section further or (2) move on to the next section.


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About the Author

GERHARD MICHAL, PhD, has retired from research at Boehringer Mannheim GmbH (now Roche Diagnostics). He is internationally acclaimed for developing the "Biochemical Pathways" wall chart. The first edition, which was published some forty years ago, has been continuously updated and is used in many biochemistry laboratories around the world.

DIETMAR SCHOMBURG, PhD, is a Full Professor and Head of the Department of Bioinformatics and Biochemistry at the Technische Universität Carolo-Wilhelmina in Braunschweig. His research interests include protein structure and function, structural biochemistry, bioinformatics, and enzyme information/metabolic networks. Dr. Schomburg has been widely praised for establishing BRENDA, the principal source of enzyme function and property data.

1. Introduction

Human immunodeficiency type 1 (HIV-1) Gag (Bell and Lever, 2013) is a multidomain protein, which contains (from the N- to C-terminus): matrix (MA), capsid (CA), spacer peptide 1 (SP1), nucleocapsid (NC, also referred to as NCp7), SP2, and p6 ( Fig. 1A ) (Henderson et al., 1992 Mervis et al., 1988). During or shortly after budding of virus particles from the infected cell, maturation occurs and the viral protease (PR) cleaves Gag at specific sites in an ordered and sequential manner to generate the mature virus structural proteins (Adamson and Freed, 2007 Ganser-Pornillos et al., 2008 Lee et al., 2012 Swanstrom and Wills, 1997). The initial Gag cleavage event yields two products: (N-terminal) MA-CA-SP1 and (C-terminal) NCp7-SP2-p6, referred to as NCp15. Further PR cleavage of NCp15 releases NCp9 (NCp7-SP2) and p6 and in the final cleavage step, processing of NCp9 produces the mature NCp7 protein and SP2 ( Fig. 1A ).

Schematic representation of NC proteins and RNA templates used in this study. (A) Proteins produced by C-terminal cleavage of Gag. HIV-1 Gag is shown with each domain indicated by rectangles depicted as follows: MA, open CA, dark gray spacer peptide 1 (SP1), open NCp7, closed SP2, open p6, light gray. The proteins derived from the Gag C-terminus, i.e., NCp15, NCp9, p6, NCp7, and SP2, are also shown. The red arrows labeled 1, 2, and 3 refer to the primary, secondary, and tertiary PR cleavages at the C-terminus of Gag (Swanstrom and Wills, 1997). (B), (C), and (D) Sequence of RNA templates and secondary structure, based on mFold analysis (Zuker, 2003): (B), RNA 200 (C), RNA 105 (D), RNA 60. Two major structural elements, i.e., the TAR and Poly A stem-loops, are present only in RNA 200. The other two templates contain varying amounts of sequence upstream of the PBS and in each case, the PBS is largely unpaired. RNA 105 also has unpaired bases downstream of the PBS in addition to a short 10-bp stem formed with bases upstream and downstream of the PBS. The PBS sequence in each template is highlighted in red. The predicted ΔG values are shown beneath the structures. The diagrams are not drawn to scale.

NCp7 is a small, basic nucleic acid binding protein containing two zinc-binding domains, i.e., zinc fingers (ZFs), each with the invariant CCHC motif, which are connected by a short basic linker peptide (Darlix et al., 2011 Darlix et al., 1995 Levin et al., 2005 Levin et al., 2010 Rein et al., 1998 Thomas and Gorelick, 2008). NCp7 and the NC domain in Gag are essential for multiple events in the virus life cycle including viral RNA dimerization and packaging, virus assembly, reverse transcription, and integration (reviewed in Darlix et al., 2011 Isel et al., 2010 Levin et al., 2005 Levin et al., 2010 Lyonnais et al., 2013 Mirambeau et al., 2010 Piekna-Przybylska and Bambara, 2011 Rein et al., 1998 Sleiman et al., 2012 Thomas and Gorelick, 2008). Importantly, NCp7 is a nucleic acid chaperone, i.e., it remodels nucleic acid structures to form the most thermodynamically stable conformations (Tsuchihashi and Brown, 1994) (reviewed in Darlix et al., 2011 Godet and Mély, 2010 Levin et al., 2005 Levin et al., 2010 Rein et al., 1998) (also see more recent refs. Hergott et al., 2013 Mitra et al., 2013 Wu et al., 2013 Wu et al., 2014). Effective chaperone activity depends on three properties: (i) aggregation of nucleic acids, which is important for annealing (associated with the basic residues) (ii) moderate duplex destabilizing activity (associated with the ZFs) and (iii) rapid on-off nucleic acid binding kinetics (Cruceanu et al., 2006a) (reviewed in Levin et al., 2005 Levin et al., 2010 Mirambeau et al., 2010 Wu et al., 2010a). This activity plays a critical role in ensuring specific and efficient reverse transcription and mediates primer placement, i.e., annealing of the tRNA Lys3 primer to the viral RNA genome, synthesis of (-) strong-stop DNA [(-) SSDNA]), and minus- and plus-strand transfer (Levin et al., 2005 Levin et al., 2010).

In addition to studies on the mature NC protein, the biological activity of the immediate NCp7 precursors, NCp15 and NCp9, has also been investigated. Under normal conditions, mature, infectious HIV-1 virions do not contain NCp15 and NCp9, which are transient intermediates in the virus assembly pathway (Henderson et al., 1992). In fact, blocking both C-terminal cleavage sites in Gag required for NCp15 processing, abolishes viral infectivity (Coren et al., 2007 de Marco et al., 2012) and results in assembly of virions with abnormal morphology (de Marco et al., 2012). If the cleavage site between NCp7 and SP2 is blocked giving rise to NCp9, there is some reduction (< 2-fold) in the number of particles that exhibit WT morphology (de Marco et al., 2012 Ohishi et al., 2011), but there is no clear consensus as to whether mutant virions are infectious, possibly due to differences in the constructs used or the different mutations used to maintain NCp9. For example, in one study it was reported that NCp9 mutants produced very little early viral DNA (㰐%), implying that the virions were replication-negative (Ohishi et al., 2011), and in another, it was shown that blocking release of SP2 completely abolished replication (Kafaie et al., 2009). In contrast, other investigators have observed that NCp9 mutant virions were infectious in a single-cycle assay (Briggs and Kräusslich, 2011 Coren et al., 2007 Müller et al., 2009). However, in one study it was found that after four weeks in cell culture, normal processing was restored and the particles contained NCp7 instead of NCp9 (Coren et al., 2007). Studies on the behavior of NCp15 and NCp9 in several different experimental contexts, e.g., single-molecule DNA stretching (Cruceanu et al., 2006b), electron microscopic imaging of NC-DNA complexes (Mirambeau et al., 2007), biophysical and biochemical analysis of nucleic acid interactions (Wang et al., 2014), and formation of genomic RNA dimers (Jalalirad and Laughrea, 2010 Kafaie et al., 2009 Ohishi et al., 2011) showed differences between the two precursors and NCp7. However, until now, a detailed biochemical analysis comparing the nucleic acid chaperone activities of the three proteins in reverse transcription has not been reported.

In the present study, we focus on the chaperone functions of NCp15, NCp9, and NCp7, using reconstituted systems that model authentic early reverse transcription events: (i) primer placement and synthesis of (-) SSDNA and (ii) minus-strand transfer. Both of these systems provide a sensitive readout for chaperone activity, but in one case (primer placement and (-) SSDNA synthesis), the system is driven by RNA-RNA interactions, whereas in the other (strand transfer), by RNA-DNA interactions (Levin et al., 2005 Levin et al., 2010). We demonstrate that of the three NC proteins, NCp9 has the greatest activity in these assays at low protein concentrations, but at higher concentrations, reverse transcriptase (RT)-catalyzed elongation is inhibited. This inhibitory effect is consistent with NCp9's slow dissociation kinetics (Cruceanu et al., 2006b Wang et al., 2014) and strong nucleic acid binding activity, which reflects the presence of its highly basic SP2 domain. In addition, we show that the presence of acidic residues in the p6 domain of NCp15 negatively impacts nucleic acid chaperone activity in DNA synthesis reactions. Collectively, our results help to explain why fully processed NCp7 has evolved as the critical cofactor for HIV-1 reverse transcription, replication, and optimal viral fitness.


By using different spectroscopic biophysical (CD and NMR) and biochemical approaches (PSAs, EMSAs and unwinding PAGE assays) we have gathered substantial evidences indicating that CNBP promotes the unfolding of G4-DNA secondary structures. CNBP primary structure agrees with its function over G4 motifs. CNBP contains seven tandem cysteine-cysteine-histidine-cysteine (CCHC) zinc-knuckle repeats and a glycine/arginine-rich region in the linker joining the first and second CCHC zinc knuckles highly similar to the arginine-glycine-glycine (RGG) box ( 14). CCHC found in CNBP are remarkably similar to those found in the human immunodeficiency virus type 1 nucleocapsid protein (HIV1-NCp) involved in G4 binding and unfolding ( 52). Additionally, R/G-rich region has been reported as an RNA binding motif involved in G4 recognition and resolution ( 53), and has recently been defined as a novel interesting quadruplex interacting (NIQI) motif shared among G4 binding proteins ( 54).

At least two different thermodynamically and kinetically driven mechanisms of action may explain the CNBP G4-unfolding activity. One of them is supported by data gathered studying intramolecular G4s formed in the PPRs of certain oncogenes and of the NOG/nog3 genes. These data suggest that, in a similar fashion than some telomere binding proteins ( 55), CNBP promote G4s unfolding by shifting the G4—single-stranded equilibrium towards the unfolded state through preferentially binding to the unfolded sequence, thus avoiding G4 re-folding ( Supplementary Figure S15 , blue arrow). The second CNBP way of action is supported by the finding that CNBP promotes the unfolding of the tetramolecular (TG4T)4, but does not stably bind to the TG4T strand. Thereby, CNBP could unfold the G4 core structure by destabilizing the central tetrads, thus driving to intermediate species prior to the full G4 disassembly. In contrast to (TG4T)4, the biologically relevant intramolecular G4s assayed in this work contain unpaired flanking sequences and interconnecting loops of variable length and base composition. Therefore, CNBP action over G4s in gene contexts may involve the preferential binding to the unfolded single stranded DNA of G4s loops/flanking sequences, the unfolding of the G4-core and the prevention of G4 refolding by stably binding to the unfolded G-rich sequence ( Supplementary Figure S15 , green arrow). Indeed, CNBP interaction with loops/flanking sequences could account for the differences in CNBP concentration required for the unfolding of the different assessed G4s. As observed from CD, PSA and EMSA data, G4 presenting the higher intrinsic stabilities required higher CNBP concentrations to be unfolded and had the lowest protein binding affinities ( Supplementary Table S2 ). Importantly, both mechanisms may not be mutually exclusive and may cooperate to achieve appropriate G4-unfolding activity on intramolecular G4s.

All G4-helicases reported so far use the energy of ATP hydrolysis to resolve the G4 structure ( 12) however, CNBP unwinds G4s in an ATP-independently manner. Consequently, CNBP should be grouped with other nucleic acid chaperones that unfold G4s independently of ATP, such as hnRNP A, described as participating in KRAS transcriptional control and several other processes concerning G4s, or Replication Protein A (RPA), involved in DNA replication, repair and recombination ( 12, 55).

High levels of CNBP have been associated with cell proliferation and survival control ( 49), but the molecular bases of this behavior remain unclear. c-MYC has been largely reported as a target of CNBP regulation and is a paradigmatic case of G4-mediated transcriptional control. Despite results obtained here did not show a transcriptional control of endogenous c-MYC encoded in genomic DNA, this regulation was evident when using a plasmid encoding a reporter gene controlled by an 850 bp-region of the c-MYC promoter that comprises the PQS. Differences between the results from experiments using reporter genes controlled by c-MYC promoter fragments and experiments assaying the transcription of endogenous c-MYC may be consequence of the complexity of c-MYC promoter ( 56). The use of fragments of such a complex promoter could lead to the loss of control elements acting in cis together with NHE III1 in the c-MYC transcriptional regulation. Moreover, we found that CNBP enhances in cellulo the transcription of the endogenous KRAS oncogene, in agreement with effects of CNBP observed in vitro over sequences representing the PQS found in KRAS PPR. KRAS PPR contains an NHE essential for transcription regulation. This region comprises a G-rich strand able to fold as G4, which was reported as responsible for gene silencing ( 43, 57). The hnRNP A1 unfolds the KRAS-G4 facilitating the pairing of the NHE strands into the duplex, thereby favoring transcription activation ( 58). Recently, high mobility group box protein 1 (HMGB1) has been reported to stabilize the KRAS-G4 acting as a transcriptional repressor ( 59). Therefore, CNBP may be a trans-acting factor involved in KRAS transcriptional regulation cooperating with hnRNP A1 and/or antagonizing with HMGB1. Mutations in KRAS occur in 75–90% of in pancreatic ductal adenocarcinoma (PDAC, OMIM # 260350), representing the most frequent, as well as the earliest, genetic alteration leading to constitutive activation of downstream signaling pathways that are important for tumor initiation, development and spread ( 60). On the other hand, CNBP has been classified as a gene related with cancer and diseases in the Human Protein Atlas ( 61) and was found as an unfavorable prognostic marker in PDAC ( 62). Considering these facts, it is tempting to speculate about a role of CNBP in PDAC through G4-mediated transcriptional activation of KRAS. Collectively, data lead us to speculate that CNBP favors cell proliferation and survival, and perhaps cancer development, through a general mechanism of action over certain oncogenes which transcription is repressed by the folding of G4s in their promoters.

The best documented biological function assigned to CNBP is the participation in the development of embryonic neurocranium ( 14, 24, 25, 63). Despite the role of CNBP in embryonic development has been reported several years ago, the molecular mechanisms underlying the role of CNBP in rostral development remain unclear. In cellulo and in vivo experiments carried out in this work have demonstrated that CNBP represses the expression of NOG/nog3 most likely through the unfolding of G4 structures reported as transcriptional enhancers ( 6). Bearing in mind that c-MYC and NOG are genes involved in neural crest formation and craniofacial development ( 51, 64, 65), it is tempting to speculate that the role of CNBP in embryonic development is sustained, at least in part, by its capability to unfold G4 structures.

The role of G4 structures on transcription could be either stimulatory (acting as DNA binding sites for regulatory factors or favoring transcription re-initiation) or inhibitory (acting as barriers or disrupting a double-stranded binding site) ( 66). Here we report that the CNBP G4-unfolding activity may lead to opposite effects on the transcription of genes depending on the role of G4. Indeed, our results show that CNBP stimulates c-MYC and KRAS while represses NOG/nog3 transcription. Whatever the final effect, CNBP seems to play a critical role in the cellular machinery involved in G4s unfolding needed for proper gene transcription. In addition, results showing an increase of nuclear G4s in cells depleted of CNBP suggest that this CNBP activity may affect other target genes beyond those ones analyzed in this work. Besides, the cytoplasmic location of CNBP, along with its role in G4-RNA-mediated translational control ( 23, 31), suggest that CNBP is involved in the control of both transcription (by binding to ssDNA and unfolding G4-DNAs in the nuclei) and translation (by binding to RNA and unfolding G4-RNAs in the cytosol).

At last, data presented here add novel evidences regarding the existence and function of G4s in whole-living systems, increasing the knowledge about the biological function G4s unfolding proteins and the mechanisms underlying the regulation of genes expression through G4 structures.

A Level CIE Notes

CIE A Level Biology revision notes made for the CIE (Cambridge International Examination) exam board. This covers all the topics and modules for all specifications including 9700.

We cover all the relevant topics in the specification below:

Topic 1 – Cell Structure Revision Notes:

Topic 2 – Biological Molecules Revision Notes:

Topic 3 – Enzymes Revision Notes:

Topic 4 – Cell Membranes and Transport Revision Notes:

Topic 5 – The Mitotic Cell Cycle Revision Notes:

Topic 6 – Nucleic Acids and Protein Synthesis Revision Notes:

Topic 7 – Transport in Plants Revision Notes:

Topic 8 – Transport in Mammals Revision Notes:

Topic 9 – Gas exchange and Smoking Revision Notes:

Topic 10 – Infectious Disease Revision Notes:

Topic 11 – Immunity Revision Notes:

Topic 12 – Energy and Respiration Revision Notes:

Topic 13 – Photosynthesis Revision Notes:

Topic 14 – Homeostasis Revision Notes:

Topic 15 – Control and Co-ordination Revision Notes:

Topic 16 – Inherited Change Revision Notes:

Topic 17 – Selection and Evolution Revision Notes:

Topic 18 – Biodiversity, Classification and Conservation Revision Notes:

Terms within categories are listed alphabetically. In the Genome editing tools section, the sub-category “General” contains terms that apply to all types of genome editing tools. Additional sub-categories contain terms specific to the sub-category of genome editing technology: “CRISPR specific”, “Meganuclease specific”, “TALEN specific”, “megaTAL specific” and “ZFN specific”. A glossary listing all terms alphabetically precedes the Terms and definitions.

Term number

CRISPR associated nuclease

DNA, RNA, or epigenome edit

DNA, RNA, or epigenome intended edit

DNA, RNA, or epigenome unintended edit

genome editing target specificity

meganuclease single chain

microhomology-mediated end joining repair

non-homologous end joining

protospacer adjacent motif

repeat variable diresidue

site-directed DNA modification enzyme

trans-activating CRISPR RNA

Insights on the Nucleic Acid Amplification Detection and Diagnostics Global Market to 2027 - Key Findings and Recommendations

According to this report the global nucleic acid amplification, detection, and diagnostics market is expected to reach US$ 38,162.68 million by 2027 from US$ 14,014.59 million in 2019. The market is estimated to grow at a CAGR of 13.4% from 2020 to 2027. The report highlights trends prevailing in the global nucleic acid amplification, detection, and diagnostics market and the factors driving market along with those that act as hindrances.

Based on nucleic acid, the global nucleic acid amplification, detection, and diagnostics market is segmented into deoxyribonucleic acid (DNA) and ribonucleic acid (RNA). In 2019, the deoxyribonucleic acid (DNA) segment held the largest share of the market also, the same segment is estimated to register the highest CAGR in the market during the forecast period. Factors such as rising adoption of DNA detection and amplification for disease diagnosis are estimated to contribute to the deoxyribonucleic acid (DNA) segment growth.

The growth of the nucleic acid amplification, detection, and diagnostics market is attributed to the factors such as increasing prevalence of chronic conditions and increasing demand for accurate and modern diagnostic measures. However, lack of expertise and inadequate infrastructure in emerging countries is likely to restraint the growth of the market during the forecast period.

The emergence of Coronavirus is expected to have positive impact on the market growth. As nucleic acid related diagnostic technologies offer superior outcomes, majority of the market players are focusing on the product development equipped with nucleic acid tests. However, implementation of physical distancing policies and total shut down of businesses in order to prevent the viral infection disrupted the supply chain operations, which deterred the market growth by certain extent.

BD, bioMerieux SA, Bio-Rad Laboratories Inc., Thermo Fisher Scientific Inc., Illumina, Inc., Danaher, QIAGEN, Abbott, Meridian Bioscience, Inc., and F. Hoffmann-La Roche Ltd. are among the leading companies operating in the nucleic acid amplification, detection, and diagnostics market.

  • Save and reduce time carrying out entry-level research by identifying the growth, size, leading players and segments in the nucleic acid amplification, detection, and diagnostics market.
  • Highlights key business priorities in order to assist companies to realign their business strategies.
  • The key findings and recommendations highlight crucial progressive industry trends in the global nucleic acid amplification, detection, and diagnostics market, thereby allowing players across the value chain to develop effective long-term strategies.
  • Develop/modify business expansion plans by using substantial growth offering developed and emerging markets.
  • Scrutinize in-depth global market trends and outlook coupled with the factors driving the market, as well as those hindering it.
  • Enhance the decision-making process by understanding the strategies that underpin security interest with respect to client products, segmentation, pricing and distribution

1. Introduction
1.1 Scope of the Study
1.2 Research Report Guidance
1.3 Market Segmentation
1.3.1 Global Nucleic Acid Amplification Detection and Diagnostic Market - By Nucleic Acid
1.3.2 Global Nucleic Acid Amplification Detection and Diagnostic Market - By Process
1.3.3 Global Nucleic Acid Amplification Detection and Diagnostic Market - By Technology
1.3.4 Global Nucleic Acid Amplification Detection and Diagnostic Market - By Application
1.3.5 Global Nucleic Acid Amplification Detection and Diagnostic Market - By End User
1.3.6 Global nucleic acid amplification detection and diagnostics market - By Geography

2. Nucleic Acid Amplification Detection and Diagnostic Market - Key Takeaways

3. Research Methodology
3.1 Coverage
3.2 Secondary Research
3.3 Primary Research

4. Global Nucleic Acid Amplification Detection and Diagnostic Market - Market Landscape
4.1 Overview
4.2 PEST Analysis
4.2.1 North America - PEST Analysis
4.2.2 Europe - PEST Analysis
4.2.3 Asia Pacific - PEST Analysis
4.2.4 Middle East and Africa (MEA) - PEST Analysis
4.2.5 South and Central America (SCAM) - PEST Analysis
4.3 Expert Opinions

5. Nucleic Acid Amplification Detection and Diagnostics Market - Key Market Dynamics
5.1 Market Drivers
5.1.1 Increasing Demand for Accurate and Modern Diagnostic Measures
5.1.2 Rising Prevalence of Chronic Conditions and Infectious Diseases
5.2 Market Restraints
5.2.1 Lack of Expertise and Inadequate Infrastructure in Emerging Countries
5.3 Market Opportunities
5.3.1 Growing Investments for the Development of New Biotechnological Diagnostic Technologies
5.4 Future Trends
5.4.1 Automations in Nucleic Acid Amplification and Detection
5.5 Impact analysis

6. Nucleic Acid Amplification Detection and Diagnostic Market - Global Analysis
6.1 Global Nucleic Acid Amplification Detection and Diagnostic Market Revenue Forecast And Analysis
6.2 Global Nucleic Acid Amplification Detection and Diagnostic Market, By Geography - Forecast And Analysis
6.3 Market Positioning of Key Players

7. Nucleic Acid Amplification, Detection and Diagnostics Market Analysis - By Nucleic Acid
7.1 Overview
7.2 Nucleic Acid Amplification, Detection and Diagnostics Market Revenue Share, by Nucleic Acid (2019 and 2027)
7.3 Deoxyribonucleic Acid (DNA)
7.3.1 Overview
7.3.2 Deoxyribonucleic acid (DNA): Nucleic Acid Amplification, Detection and Diagnostics Market - Revenue and Forecast to 2027 (US$ Million)
7.4 Ribonucleic Acid (RNA)
7.4.1 Overview
7.4.2 Ribonucleic Acid (RNA): Nucleic Acid Amplification, Detection and Diagnostics Market - Revenue and Forecast to 2027 (US$ Million)

8. Nucleic Acid Amplification, Detection and Diagnostics Market Analysis - By Process
8.1 Overview
8.2 Nucleic Acid Amplification, Detection and Diagnostics Market Revenue Share, by Process (2019 and 2027)
8.3 Amplification
8.4 Detection
8.5 Diagnostics

9. Nucleic Acid Amplification, Detection and Diagnostics Market Analysis - By Product Type
9.1 Overview
9.2 Nucleic Acid Amplification, Detection and Diagnostics Market Share, by Product Type, 2019 and 2027, (%)
9.3 Assays
9.3.1 Overview
9.3.2 Assays: Nucleic Acid Amplification, Detection and Diagnostics Market - Revenue and Forecast to 2027 (US$ Million)
9.4 Kits and Reagents
9.4.1 Overview
9.4.2 Kits and Reagents: Nucleic Acid Amplification, Detection and Diagnostics Market - Revenue and Forecast to 2027 (US$ Million)
9.5 Systems
9.5.1 Overview
9.5.2 Systems: Nucleic Acid Amplification, Detection and Diagnostics Market - Revenue and Forecast to 2027 (US$ Million)

10. Nucleic Acid Amplification, Detection and Diagnostics Market Analysis - By Technology
10.1 Overview
10.2 Nucleic Acid Amplification, Detection and Diagnostics Market Share, by Technology, 2019 and 2027, (%)
10.3 Polymerase Chain Reaction (PCR)
10.5 Direct Nucleic Acid Detection
10.6 Next Generation Sequencing (NGS)

11. Nucleic Acid Amplification, Detection and Diagnostics Market Analysis - By Application
11.1 Overview
11.2 Nucleic Acid Amplification, Detection and Diagnostics Market Share, by Application, 2019 and 2027, (%)
11.3 Infectious Diseases
11.4 Genetic Diseases
11.5 Forensic Testing
11.6 Paternity Testing
11.7 Oncology
11.8 Others

12. Nucleic Acid Amplification, Detection and Diagnostics Market Analysis - By End User
12.1 Overview
12.2 Nucleic Acid Amplification, Detection and Diagnostics Market Share, by End User, 2019 and 2027, (%)
12.3 Hospital and Clinics
12.3.1 Overview
12.3.2 Hospital and Clinics: Nucleic Acid Amplification, Detection and Diagnostics Market - Revenue and Forecast to 2027 (US$ Million)
12.4 Diagnostic Centers
12.4.1 Overview
12.4.2 Diagnostic Centers: Nucleic Acid Amplification, Detection and Diagnostics Market - Revenue and Forecast to 2027 (US$ Million)
12.5 Research Institutes
12.5.1 Overview
12.5.2 Research Institutes: Nucleic Acid Amplification, Detection and Diagnostics Market - Revenue and Forecast to 2027 (US$ Million)
12.6 Others
12.6.1 Overview
12.6.2 Others: Nucleic Acid Amplification, Detection and Diagnostics Market - Revenue and Forecast to 2027 (US$ Million)

13. Nucleic Acid Amplification, Detection and Diagnostics Market Analysis and Forecasts to 2027 - Geographical Analysis
13.1 North America : Nucleic Acid Amplification, Detection and Diagnostics Market
13.2 Europe : Nucleic Acid Amplification Detection and Diagnostic Market
13.3 Asia Pacific : Nucleic Acid Amplification Detection and Diagnostic Market
13.4 Middle East & Africa : Nucleic Acid Amplification Detection and Diagnostic Market
13.5 South and Central America : Nucleic Acid Amplification, Detection and Diagnostics Market

14. Impact of COVID-19 Pandemic on Global Nucleic Acid Amplification, Detection and Diagnostics Market
14.1 North America : Impact Assessment of COVID-19 Pandemic
14.2 Europe : Impact Assessment Of COVID-19 Pandemic
14.3 Asia Pacific : Impact Assessment of COVID-19 Pandemic
14.4 Middle East and Africa : Impact Assessment of COVID-19 Pandemic
14.5 South and Central America : Impact Assessment of COVID-19 Pandemic

15. Nucleic Acid Amplification Detection and Diagnostic Market - Industry Landscape
15.1 Overview
15.2 Growth Strategies in the Nucleic Acid Amplification Detection and Diagnostic Market, 2015-2020
15.3 Inorganic Growth Strategies
15.3.1 Overview
15.4 Organic Growth Strategies
15.4.1 Overview

16. Company Profiles
16.1 BD
16.1.1 Key Facts
16.1.2 Business Description
16.1.3 Products and Services
16.1.4 Financial Overview
16.1.5 SWOT Analysis
16.1.6 Key Developments
16.2 bioMerieux SA
16.2.1 Key Facts
16.2.2 Business Description
16.2.3 Products and Services
16.2.4 Financial Overview
16.2.5 SWOT Analysis
16.2.6 Key Developments
16.3 Bio-Rad Laboratories Inc.
16.3.1 Key Facts
16.3.2 Business Description
16.3.3 Products and Services
16.3.4 Financial Overview
16.3.5 SWOT Analysis
16.3.6 Key Developments
16.4 Thermo Fisher Scientific Inc.
16.4.1 Key Facts
16.4.2 Business Description
16.4.3 Products and Services
16.4.4 Financial Overview
16.4.5 SWOT Analysis
16.4.6 Key Developments
16.5 Illumina, Inc.
16.5.1 Key Facts
16.5.2 Business Description
16.5.3 Products and Services
16.5.4 Financial Overview
16.5.5 SWOT Analysis
16.5.6 Key Developments
16.6 Danaher
16.6.1 Key Facts
16.6.2 Business Description
16.6.3 Products and Services
16.6.4 Financial Overview
16.6.5 SWOT Analysis
16.6.6 Key Developments
16.7.1 Key Facts
16.7.2 Business Description
16.7.3 Products and Services
16.7.4 Financial Overview
16.7.5 SWOT Analysis
16.7.6 Key Developments
16.8 Abbott
16.8.1 Key Facts
16.8.2 Business Description
16.8.3 Products and Services
16.8.4 Financial Overview
16.8.5 SWOT Analysis
16.8.6 Key Developments
16.9 Meridian Bioscience, Inc.
16.9.1 Key Facts
16.9.2 Business Description
16.9.3 Products and Services
16.9.4 Financial Overview
16.9.5 SWOT Analysis
16.9.6 Key Developments
16.10 F. Hoffmann-La Roche Ltd.
16.10.1 Key Facts
16.10.2 Business Description
16.10.3 Products and Services
16.10.4 Financial Overview
16.10.5 SWOT Analysis
16.10.6 Key Developments

17. Appendix
17.1 About the Publisher
17.2 Glossary of Terms

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3. Agents for Targeting of dsDNAs

3.1. TINA-Modified Triplex Forming Oligonucleotides

3.2. Invader Probes

30–50 min in medium salt buffer containing 110 mM Na + , pH = 7.0 at 20 °C), the recognition can be easily monitored in real time by the decrease of excimer fluorescence of the Invader LNA probe [237]. Although, due to difficult and insufficient multistep synthesis of the pyrene-modified LNA monomer L1, the Invader LNA probes have not been further developed.

20/30/55 pM, respectively [57]. At the same time, the possibility of the visualization of an unique region within the DYZ-1 satellite (

6 × 10 4 repeats) on the bovine ( Bos taurus ) Y chromosome using 5′-Cy3-labeled Invader probes modified by three arrangements of monomer K4 has been demonstrated in conditions of non-denaturating FISH experiments [56].

100-fold excess of the probe). However, 14-mer probes with the three +1 zipper motifs demonstrate lower recognition of dsDNA (

125-fold excess of the probe). The authors of [59] have shown that the modification of the Invader probes architecture with non-nucleosidic nonyl (C9-linker) bulge insertions leads to more affine, faster, and more persistent dsDNA recognition (relative to conventional Invader probes).

Watch the video: μάθημα 38 Κυτταρική Διαίρεση, Μίτωση part 4. Βιολογία Γ λυκείου, Biology maniax (October 2022).