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El. knyga: Chemical Reagents for Protein Modification: 2nd Edition

(Lundblad Biotechnology, Chapel Hill, North Carolina, USA)
  • Formatas: 352 pages
  • Serija: Routledge Revivals
  • Išleidimo metai: 11-Mar-2020
  • Leidėjas: CRC Press
  • Kalba: eng
  • ISBN-13: 9781000694710
Kitos knygos pagal šią temą:
  • Formatas: 352 pages
  • Serija: Routledge Revivals
  • Išleidimo metai: 11-Mar-2020
  • Leidėjas: CRC Press
  • Kalba: eng
  • ISBN-13: 9781000694710
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First published in 1991, Chemical Reagents for Protein Modification, 2nd Edition provides a unique combination of theoretical and practical considerations for the use of chemical reagents for site-specific modification of proteins. The book is divided into three sections, with the first section describing general techniques, including information on the organic chemistry of the various modification reactions; the separation and characterization of site-specific modified proteins, including applications to proteins separated by electrophoresis followed by blotting; the specific chemical cleavage of peptide bonds in proteins; the separation of peptides by high-performance liquid chromatography and electrophoresis; and the use of chemical reagents to assess conformational change in proteins.

The second section provides an encyclopedic description of reagents and reactions for the site-specific modification of individual amino acid residues in proteins. The final section presents descriptions of the use of chemical reagents to label biologically significant sites in proteins, including enzyme active sites and the use of covalent cross-linking to measure protein-protein interactions. Particular emphasis is placed on the use of photoaffinity reagents. The book will be an extremely useful research tool for all investigators interested in the solution chemistry of proteins.
1. Site-Specific Chemical Modification of Proteins.
2. Amino Acid
Analysis.
3. Peptide Separation by Reverse-Phase High-Performance Liquid
Chromatography.
4. Methods for Sequence Determination.
5. Chemical Cleavage
of Peptide Bonds.
6. The Modification of Cysteine.
7. The Modification of
Cysteine Cleavage of Disulfide Bonds.
8. The Modification of Methionine.
9.
The Modification of Histidine Residues.
10. The Modification of Lysine.
11.
The Modification of Arginine.
12. Chemical Modification of Tryptophan.
13.
The Modification of Tyrosine.
14. The Modification of Carboxyl Groups.
15.
The Chemical Cross-Linking of Peptide Chains.
16. Affinity Labeling. Index.
Roger L. Lundblad