Side-chain structure and dynamics at the lipid-protein interface: Val1 of the gramicidin A channel.

Abstract:

:High resolution dynamics and structural information has been resolved from 2H solid-state NMR spectra of the Val-1 side-chain of the gramicidin channel in a lipid bilayer. Both powder pattern lineshapes and spectra from uniformly aligned samples of gramicidin in lipid bilayers have been analyzed to achieve a fully consistant interpretation of the data. Torsional motions about the C alpha C beta axis (chi 1) are shown to be three-state jumps in which the occupancy of the states is given by the ratio, 75:15:10 for the chi 1 angles of 184 degrees:304 degrees:64 degrees. The dominant conformer is also the most common conformation observed for valines in well defined protein structures. The distribution of conformational substates that represents the chi 1 dynamics appears to be largely independent of the lipid phase transition and the hydration of the sample. However, there is evidence that the residence time between jumps is dependent on the lipid phase transition. Although this time is shown to be approximately 1 microseconds below the phase transition temperature, it is in the fast exchange limit above the transition temperature.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Lee KC,Cross TA

doi

10.1016/S0006-3495(94)80928-2

subject

Has Abstract

pub_date

1994-05-01 00:00:00

pages

1380-7

issue

5

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(94)80928-2

journal_volume

66

pub_type

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