Significance of bound water to local chain conformations in protein crystals.

Abstract:

:We examine how the polypeptide chain in protein crystal structures exploits the multivalent hydrogen-bonding potential of bound water molecules. This shows that multiple interactions with a single water molecule tend to occur locally along the chain. A distinctive internal-coordinate representation of the local water-binding segments reveals several consensus conformations. The fractional water occupancy of each was found by comparison of the total number of conformations in the database regardless of the presence or absence of bound water. The water molecule appears particularly frequently in type II beta-turn geometries and an N-terminal helix feature. This work constitutes a first step into assessing not only the generality but also the significance of specific water binding in globular proteins.

authors

Robert CH,Ho PS

doi

10.1073/pnas.92.16.7600

keywords:

subject

Has Abstract

pub_date

1995-08-01 00:00:00

pages

7600-4

issue

16

eissn

0027-8424

issn

1091-6490

journal_volume

92

pub_type

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