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By Shan S. Wong
Since the ebook of the 1st version of Chemistry of Protein Conjugation and Cross-Linking in 1991, new cross-linking reagents, significantly multifunctional cross-linkers, were constructed and synthesized. The final touch of the human genome venture has opened a brand new quarter for learning nucleic acid and protein interactions utilizing nucleic acid cross-linking reagents, and advances have additionally been made within the quarter of biosensors and microarray biochips for the detection and research of genes, proteins, and carbohydrates. additionally, advancements in actual recommendations with unheard of sensitivity and determination have facilitated the research of cross-linked items.
Updated to mirror the advances of the twenty first century, this ebook offers:
- An assessment of the chemical ideas underlying the procedures of cross-linking and conjugation
- A thorough checklist of cross-linking reagents released within the literature because the first version, protecting monofunctional, homobifunctional, heterobifunctional, multifunctional, and zero-length cross-linkers
- Reviews of using those reagents in learning protein tertiary buildings, geometric preparations of subunits inside advanced proteins and nucleic acids, near-neighbor research, protein-to-protein or ligand–receptor interactions, and conformational adjustments of biomolecules
- Discusses the appliance of immunoconjugation for immunoassays, immunotoxins for designated remedy, microarray know-how for research of assorted biomolecules, and strong kingdom chemistry for immobilizations
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Extra resources for Chemistry of Protein and Nucleic Acid Cross-Linking and Conjugation
Example text
In still other cases, functional groups are converted into one another to either change their specificity or increase their reactivity. The importance of these manipulations is clearly demonstrated by many examples found in the literature. 1 Reduction of Disulfide Bonds Disulfide bonds formed from two cysteine residues cross-link two portions of a protein where these amino acids are located. This oxidized form of sulfur is relatively unreactive but can be easily activated by reduction to free sulfhydryl groups.
28. Lundblad, R. L. and Noyes, C. , Chemical Reagents for Protein Modification, Vol. I, CRC Press, Boca Raton, FL, 1984, p. 16. 29. Tanford, C. and Hauenstein, J. , Hydrogen-ion equilibriums of ribonuclease, J. Am. Chem. , 78, 5287, 1956. 32 Chemistry of Protein and Nucleic Acid Cross-Linking and Conjugation 30. Haschemeyer, R. H. and Haschemeyer, A. E. , Proteins: A Guide to Study by Physical and Chemical Methods, Wiley-Interscience, New York, 1973. 31. , Serine proteases: Structure and mechanism of catalysis, Annu.
Imidazole catalysis. IV. The reaction of general bases with p-nitrophenyl acetate in aqueous solution, J. Am. Chem. , 80, 2265, 1958. 19. Freedman, R. B. and Radda, G. , The reaction of 2,4,6-trinitrobenzeuesulfonic acid with amino acids, peptides, and proteins, Biochem. , 108, 383, 1968. 20. Hudson, R. , Nucleophilic reactivity, in Chemical Reactivity and Reaction Paths, Klopman, G. ), John Wiley & Sons, New York, 1974, Chapter 5. 21. Stark, G. , Reactions of cyanate with functional groups of proteins.