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The hydration of protein secondary structures
Author(s) -
Barlow D.J.,
Poole P.L.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81535-1
Subject(s) - protein secondary structure , crystallography , chemistry , crystal structure , protein structure , infrared spectroscopy , biochemistry , organic chemistry
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 β‐sheet proteins compared with α‐helical ones. Analysis of the protein crystal structures shows that this is due primarily to differences in the geometry ofwater‐CO group interactions in the two types of secondary structure.