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Protein Stability and Folding Supplement 1 A Collection of Thermodynamic Data by Wolfgang Pfeil

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Published by Springer Berlin Heidelberg, Imprint, Springer in Berlin, Heidelberg .
Written in English


Book details:

Edition Notes

Statementby Wolfgang Pfeil
The Physical Object
Format[electronic resource] :
Pagination1 online resource (XIII, 521 pages 1 illustration)
Number of Pages521
ID Numbers
Open LibraryOL27083507M
ISBN 103642564623
ISBN 109783642564628
OCLC/WorldCa840292209

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Dec 18,  · The second chapter deals with the chemical stability of proteins and the pathways by which their covalent structure can degrade. The remainder of the book is devoted to techniques used in the study of these two major areas of protein stability, as well as several areas of active lfcmalta.com by: The second chapter deals with the chemical stability of proteins and the pathways by which their covalent structure can degrade. The remainder of the book is devoted to techniques used in the study of these two major areas of protein stability, as well as several areas of active research. Jan 20,  · The first part explains the principles and factors governing protein stability, and how this knowledge may be used to predict folding pathways. It also surveys important techniques used to study the protein folding process, including spectroscopic, chemical and biological techniques. The intent of this work is to bring together in a single volume the techniques that are most widely used in the study of protein stability and protein folding. Over the last decade our understanding of how p- teins fold and what makes the folded conformation stable has advanced rapidly. The.

Unique in its powerful combination of theory and practice, Protein Structure, Stability, and Folding offers protein and biophysical chemists the means to gain a more comprehensive understanding of this complex area by detailing many of the major innovative techniques in use today. As architecture needs static calculations, protein structure is always related to thermodynamic factors that govern folding and stability of a particular folded protein over the non-organized polypeptide chain. During the past decades a huge amount of thermodynamic data related to Author: Wolfgang Pfeil. Protein Folding aims to collect the most important information in the field of protein folding and probes the main principles that govern formation of the three-dimensional structure of a protein from a nascent polypeptide chain, as well as how the functional properties appear. The first part explains the principles and factors governing protein stability, and how this knowledge may be used to predict folding pathways. It also surveys important techniques used to study the protein folding process, including spectroscopic, chemical and biological techniques.

However, from recent studies (Pace) of mutant proteins made through site-specific mutagenesis, it appears that H bonds contribute significantly to protein folding and stability, and may make a greater contribution to stability of the native state than the hydrophobic effect. The main factor which opposes folding is chain conformational entropy. The intent of this work is to bring together in a single volume the techniques that are most widely used in the study of protein stability and protein folding. The handling of modern proteins is difficult due to problems with stability. This collection gives protein stability data for various temperatures and solvents, for use in the developing of protein Read more. The large number of weak hydrogen bonds within a polypeptide and between polypeptides adds up to a collectively strong force that promotes protein folding and stability.