Chemical Reagents for Protein Modification

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A01=Roger L. Lundblad
Acetic Anhydride
acid
acids
Active Site Histidine
advanced chemical biology
Afnity Labels
Alkylation
amino
amino acid residue analysis
Arginyl Residues
Author_Roger L. Lundblad
bioconjugate synthesis methods
bond
Category=PSB
Chemical modification of proteins
Citraconic Anhydride
CNBr
Cyanogen Bromide Cleavage
cysteine
Cysteine Sulfenic Acid
Cysteinyl Residues
disulde
Disulde Bond
Disulde Bond Reduction
eq_bestseller
eq_isMigrated=1
eq_isMigrated=2
eq_nobargain
eq_non-fiction
eq_science
histidine
Histidine Residues
ICAT
iodoacetic
Mixed Disulde
MMTS
Molar Excess
Native Chemical Ligation
Nitration
Oxidation
Peroxynitrous Acid
post-translational modification
protein labeling techniques
proteomics experimental protocols
Reduction
Reductive Alkylation
residue
residues
site-specific protein modification strategies
Sodium Cyanoborohydride
Streptococcal Proteinase
Succinic Anhydride
Sulfhydryl Groups
Tandem Mass Tag
Tyrosyl Residues

Product details

  • ISBN 9780367659165
  • Weight: 1188g
  • Dimensions: 178 x 254mm
  • Publication Date: 30 Mar 2021
  • Publisher: Taylor & Francis Ltd
  • Publication City/Country: GB
  • Product Form: Paperback
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The use of the chemical modification of proteins has evolved over the past 80 years, benefiting from advances in analytical, physical, and organic chemistry. Over the past 30 years, the use of chemical reagents to modify proteins has been crucial in determining the function and structure of purified proteins. This groundbreaking work is part of the foundation of emerging disciplines of proteomics, chemical biology, structure biology, and chemical proteomics.

Chemical Reagents for Protein Modification, Fourth Edition provides a comprehensive review of reagents used for the chemical modification of proteins, representing a major revision of the work presented in previous editions. The completely updated Fourth Edition is substantially larger and includes five new chapters:



  • Alkylating Agents


  • Acylating Agents


  • Nitration and Nitrosylation


  • Oxidation


  • Modification of Proteins with Reducing Agents


There is greatly increased coverage of the chemical modification of cysteine, which is critical for bioconjugate synthesis. The chapter on reduction also provides information necessary for bioconjugate synthesis as well as for the processing of inclusion bodies. The book places emphasis on conditions that affect the specificity of the chemical modification of proteins, such as solvent and temperature. The format has been markedly revised, presenting information based on the chemical nature of the modifying material and on the amino acid residue modified. This new version has increased significance to biopharmaceuticals. Much of the information is in tabular form, which enables the rapid location of cited material.

Roger L. Lundblad is a native of San Francisco, California. He received his undergraduate education at Pacific Lutheran University and his PhD in biochemistry from the University of Washington. After his postdoctoral work in the laboratories of Stanford Moore and William Stein at The Rockefeller University, he joined the faculty of the University of North Carolina at Chapel Hill. He then joined the Hyland Division of Baxter Healthcare in 1990. Currently, Dr. Lundblad works as an independent consultant at Chapel Hill, North Carolina, and writes on biotechnological issues. He is an adjunct professor of pathology at the University of North Carolina at Chapel Hill.

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