Protein Structure
Thomas E. Creighton(Author)
Oxford University Press
Published on 1. April 1989
Book
Paperback/Softback
370 pages
978-0-19-963000-4 (ISBN)
Article exhausted; check for reprint
Description
Collecting together a range of methods likely to be useful in most biochemical laboratories, this book gives techniques for protein structure studies, which allow a low-resolution picture of a protein to be built up. More detailed methods for investigations of function can be found in the companion volume also edited by Thomas Creighton, "Protein Function: A Practical Approach".
More details
Edition
New edition
Language
English
Place of publication
Oxford
United Kingdom
Target group
College/higher education
Professional and scholarly
Edition type
New edition
Illustrations
83 line drawings, 23 half-tones, index
ISBN-13
978-0-19-963000-4 (9780199630004)
Copyright in bibliographic data is held by Nielsen Book Services Limited or its licensors: all rights reserved.
Schweitzer Classification
Other editions
New editions
Creighton
Protein Structure
Book
03/1997
2nd Edition
Oxford University Press
€37.08
Article exhausted; check different version
Content
Estimating molecular weights of polypeptides by SDS Gel electrophoresis; isoelectric focusing of proteins in conventional and immobilized pH gradients, Righetti; two-dimensional polyacrylamide gel electrophoresis of prteins, Strahler; immunological detection of proteins of known sequence, Scheidtmann; peptide mapping, Carrey; counting integral numbers of residues by chemical modification, Hollecker; disulphide bonda between cysteine residues, Creighton; predictions of protein structure from gene and amino acid sequences, Argos; folding proteins, Jaenicke; analysis of protein conformation by gel electrophoresis, Goldenberg; spectral methods of characterizing protein conformation and conformational changes, Schmid; immunochemical analysis of protein conformation, Friguet; measuring the conformational stability of a protein, Pace; stabilization of protein structure by solvents, Timasheff; minimizing irreversible modification of proteins, Volkin.