Literature DB >> 3556589

The hydration of protein secondary structures.

D J Barlow, P L Poole.   

Abstract

The hydration of the main-chain carbonyl (CO) groups in proteins have been studied using infra-red spectroscopy, and computer-graphics analysis of high resolution protein crystal structures. The IR measurements indicate that the strength of water binding to the CO groups is lower in beta-sheet proteins compared with alpha-helical ones. Analysis of the protein crystal structures shows that this is due primarily to differences in the geometry of water-CO group interactions in the two types of secondary structure.

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Year:  1987        PMID: 3556589     DOI: 10.1016/0014-5793(87)81535-1

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers.

Authors:  S J Prestrelski; N Tedeschi; T Arakawa; J F Carpenter
Journal:  Biophys J       Date:  1993-08       Impact factor: 4.033

2.  Lyophilization-induced reversible changes in the secondary structure of proteins.

Authors:  K Griebenow; A M Klibanov
Journal:  Proc Natl Acad Sci U S A       Date:  1995-11-21       Impact factor: 11.205

3.  Dried Protein Structure Revealed at the Residue Level by Liquid-Observed Vapor Exchange NMR.

Authors:  Candice J Crilly; Julia A Brom; Mark E Kowalewski; Samantha Piszkiewicz; Gary J Pielak
Journal:  Biochemistry       Date:  2021-01-05       Impact factor: 3.162

  3 in total

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