Methods in Protein Folding
Wiley-VCH (Publisher)
1st Edition
Published on 9. November 2015
Book
Paperback/Softback
400 pages
978-3-527-31777-6 (ISBN)
Description
This is a unique collection of tried-and-tested laboratory protocols and method descriptions showing how to study protein folding in both the test tube and in the living cell. Expert authors share their experience of sometimes-difficult techniques and provide valuable hints on how to improve the performance of each method. More than 150 detailed protocols from the repertoire of biophysics, biochemistry and molecular biology are included, making this the single most comprehensive 'cookbook' for protein researchers.
More details
Edition
1. Auflage
Language
English
Place of publication
Weinheim
Germany
Target group
Professional and scholarly
Dimensions
Height: 240 mm
Width: 170 mm
ISBN-13
978-3-527-31777-6 (9783527317776)
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Schweitzer Classification
Persons
Johannes Buchner holds the chair of Biotechnology at the Technical University of Munich (Germany). He studied Biology at the University of Regensburg and afterwards joined the group of Ira Pastan at the National Cancer Institute in Bethesda (United States). Returning to Germany, he took a up junior group leader position at Regensburg before becoming full professor at Munich in 1998. Professor Buchner's research is centered on the folding process of proteins and its efficiency in vitro and in vivo. To improve the efficiency of protein production, he has pioneered the biotechnological use of chaperones and holds several patents in this area of research. Thomas Kiefhaber is Professor of Biophysical Chemistry at the Biozentrum, University of Basel (Switzerland). He studied Biology at the University of Regensburg (Germany) and, after completing his PhD in Biophysical Chemistry, spent two years as a post-doc with R. L. Baldwin at Stanford University. Since 1993 he is a member of the faculty of Basel University and was named professor for Biophysical Chemistry in 1999. Professor Kiefhaber's research is centered on the investigation of kinetics and mechanism of protein folding with biophysical methods.
Content
BIOPHYSICAL AND COMPUTATIONAL METHODS Prediction of protein free energy and stability Spectroscopic techniques to study protein stability and folding Protein denaturation by chaotropic agents Calorimetry of protein folding and unfolding MRD studies of protein conformation Fast relaxation methods NMR studies of protein folding kinetics FRET measurements to determine intramolecular distances Isotopic methods Laser light scattering to study protein aggregation Methods to study oligomer formation Methods to study the folding of membrane proteins MD simulation of protein folding MOLECULAR AND CELL BIOLOGY METHODS In vivo labeling of proteins Measuring chaperone activity In vivo measuring of protein fiber assembly In vivo spectroscopic methods Measurement of disulfide bond formation Enzymatic catalysis of prolyl isomerization In vitro reconstitution of folding complexes Analysis of protein folding in the ER Analysis of glycoproteins Mutational analysis of chaperones in yeast Genetic assays for protein folding Measurement of protein translocation across membranes In vitro and in vivo measurement of prion activity (partial contents)