Physics of protein structure and dynamics : when and why proteins fold or don't fold /

Looks at various aspects of protein structure and dynamics from a physico-chemical point of view. It goes into some depth regarding the description of non-covalent forces that determine the relative stability of folded and unfolded proteins. Anharmonic protein dynamics involving motions between diff...

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1. Verfasser: Schweitzer-Stenner, Reinhard (VerfasserIn)
Format: Elektronisch E-Book
Sprache:Englisch
Veröffentlicht: London, United Kingdom : Academic Press, [2025]
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Online-Zugang:ScienceDirect
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020 |a 9780443159657  |q electronic book 
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082 0 4 |a 572/.633  |2 23/eng/20241016  |1 https://id.oclc.org/worldcat/ddc/E48jGJPcFQq7YYXVwJVfPdf6F8 
100 1 |a Schweitzer-Stenner, Reinhard,  |e author.  |1 https://id.oclc.org/worldcat/entity/E39PBJc3M9gFVw3bfTPDYvBByd 
245 1 0 |a Physics of protein structure and dynamics :  |b when and why proteins fold or don't fold /  |c Reinhard Schweitzer-Stenner. 
264 1 |a London, United Kingdom :  |b Academic Press,  |c [2025] 
300 |a 1 online resource 
336 |a text  |b txt  |2 rdacontent 
337 |a computer  |b c  |2 rdamedia 
338 |a online resource  |b cr  |2 rdacarrier 
504 |a Includes bibliographical references and index. 
520 |a Looks at various aspects of protein structure and dynamics from a physico-chemical point of view. It goes into some depth regarding the description of non-covalent forces that determine the relative stability of folded and unfolded proteins. Anharmonic protein dynamics involving motions between different minima of a rugged Gibbs energy landscape is described in great detail. The book combines various aspects of the protein folding/unfolding processes with an overview of intrinsically disordered proteins, which have attracted considerable interest of the protein community over the last 25 years but are thus far underrepresented in classroom-oriented textbooks. The book looks at protein folding and intrinsically disordered proteins as heavily interrelated topics that need to be viewed together. Furthermore, it presents some basic physico-chemical aspects of protein/peptide self-assembly into nanoscale fibrils. Intrinsically disordered peptides and proteins play a major role particularly in aggregation and self-assembly processes that lead to various diseases (Alzheimer, Parkinson, Huntington, Mad-Cow). Therefore, the relevance of protein disorder for protein self-assembly deserves a closer look. Protein self-assembly cannot be separated from protein folding since it is frequently the product of misfolding. With regard to modern theories, the folding processes are linked to insights on protein dynamics and the discovered relationship between proteins and spin glasses. 
588 |a Description based on online resource; title from digital title page (viewed on March 03, 2025). 
505 8 |a 4.5 Characterizing the conformational ensembles of intrinsically disordered proteins -- 4.6 Orderdisorder and disorderdisorder transitions -- 4.7 Topics for discussion -- 4.8 Problems -- References -- 5 Protein and peptide self-assembly -- 5.1 Introduction -- 5.2 Amyloid structure and underlying forces -- 5.3 Kinetics of amyloid formation -- 5.4 Liquid-liquid demixing -- 5.5 Outlook -- 5.6 Topics of discussion -- 5.7 Problems -- References -- 6 Summary and outlook -- References -- Index -- Back Cover. 
650 0 |a Protein folding. 
650 0 |a Self-assembly (Chemistry) 
650 6 |a Protéines  |x Repliement.  |0 (CaQQLa)201-0217303 
650 6 |a Autoassemblage.  |0 (CaQQLa)201-0345487 
650 7 |a Protein folding  |2 fast  |0 (OCoLC)fst01079687 
650 7 |a Self-assembly (Chemistry)  |2 fast  |0 (OCoLC)fst01111504 
776 0 8 |c Original  |z 0443159645  |z 9780443159640  |w (OCoLC)1419058179 
856 4 0 |3 ScienceDirect  |u https://www.sciencedirect.com/science/book/9780443159640