Chemical Reagents for Protein Modification
About this book
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.
Reader Profile
· 186 pages · ≈ 3 h 27 m · Moderate
How long does it take to read Chemical Reagents for Protein Modification?
About ≈ 3 h 27 m — 186 pages, assuming roughly 250 words per page at 225 words per minute.
How many pages is Chemical Reagents for Protein Modification?
186 pages in its most-read edition.
What genre is Chemical Reagents for Protein Modification?
It sits on the Science shelves.
Is Chemical Reagents for Protein Modification in the public domain?
No — it is still under copyright.
Who wrote Chemical Reagents for Protein Modification?
Roger L. Lundblad.
“The advent of techniques such as site-specific mutagenesis (oligonucleotide-directed mutagenesis) and solution chemistry approaches such as nuclear magnetic resonance has been of great value to protein chemistry.”