Intrahelical hydrogen bonding of serine, threonine and cysteine residues within alpha-helices and its relevance to membrane-bound proteins.

Abstract:

:A survey of known protein structures reveals that approximately 70% of serine residues and at least 85% (potentially 100%) of threonine residues in helices make hydrogen bonds to carbonyl oxygen atoms in the preceding turn of the helix. The high frequency of intrahelical hydrogen bonding is of particular significance for intrinsic membrane-bound proteins that form transmembrane helices. Hydrogen bonding within a helix provides a way for serine, threonine and cysteine residues to satisfy their hydrogen-bonding potential permitting such residues to occur in helices buried within a hydrophobic milieu.

journal_name

J Mol Biol

authors

Gray TM,Matthews BW

doi

10.1016/0022-2836(84)90446-7

subject

Has Abstract

pub_date

1984-05-05 00:00:00

pages

75-81

issue

1

eissn

0022-2836

issn

1089-8638

pii

0022-2836(84)90446-7

journal_volume

175

pub_type

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