Chemical Modificatn Proteins
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Chemical Modificatn Proteins (Laboratory Techniques in Biochemistry and Molecular Biology) by A. N. Glazer

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Published by Elsevier Science & Technology .
Written in English


  • Biotechnology,
  • Chemistry,
  • Immunology,
  • Proteins,
  • Life Sciences - Biochemistry,
  • Science

Book details:

Edition Notes

ContributionsR. J. Delange (Editor)
The Physical Object
Number of Pages206
ID Numbers
Open LibraryOL10534309M
ISBN 100720442117
ISBN 109780720442113

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Chemical Modification of Proteins - Ebook written by E. Work, T. S. Work. Read this book using Google Play Books app on your PC, android, iOS devices. Download for offline reading, highlight, bookmark or take notes while you read Chemical Modification of Proteins.   Purchase Chemical Modification of Proteins, Volume 4 - 1st Edition. Print Book & E-Book. ISBN , Book Edition: 1. Revised and updated, Chemical Reagents for Protein Modification, Third Edition is an encyclopedic work describing the many approaches to the site-specific modification of proteins. More than 2, references are cited describing the development of the various by:   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 : CRC Press.

Protein Post-Translational Modification. Protein modifications performed by “extra-translational” processes. Cannot be definitively predicted from DNA sequence. Can involve very complex systems of enzymes. In some cases, “consensus” sites of modification can be identified. Ubiquitous in eukaryotes. Frequently critical for. Additional Physical Format: Online version: Means, Gary E. Chemical modification of proteins. San Francisco, Holden-Day [] (OCoLC) Document Type. Protein chemical modification is a problem-solving technique in research and technology. Modifications also occur in natural deteriorations. Generally these modifications are with the most reactive side chains and are predominantly oxidations, reductions, and nucleophilic and electrophilic substitutions. Deteriorations include peptide bond scissions, racemizations, β-eliminations, and.   First published in , 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 Cited by:

  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 theCited by: The library of chemical reactions for C–C and C–heteroatom bond formation is exceptional. The understanding of reactivity and diverse aspects of selectivity facilitates the functional group transformation of high complexity. However, the same is not valid for proteins as an organic substrate. Gratifyingly, w Organic &; Biomolecular Chemistry HOT article collection Editor’s Collection Cited by: 2. "The contents of this book are focused on the use of chemical modification to study the properties of proteins in solution. Particular emphasis has been placed on the practical laboratory aspects of this approach to the study of the relationship between structure and function in the complex class of biological heteropolymers."--Provided by publisher. "a very good reference in the area of practical protein chemistrythroughout the book there is an excellent indication of where the challenges and the trends for research are going for each particular reaction or methodologya valuable resource to get introduced to this topic and understand in depth strategies and mechanisms for modifying the surface activity of proteins.