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Asymmetric stability among the transmembrane helices of lactose permease.

Abstract:

Combining structure determinations from nuclear magnetic resonance (NMR) data and molecular dynamics simulations (MD) under the same environmental conditions revealed a startling asymmetry in the intrinsic conformational stability of secondary structure in the transmembrane domain of lactose permease (LacY). Eleven fragments, corresponding to transmembrane segments (TMs) of LacY, were synthesized, and their secondary structure in solution was determined by NMR. Eight of the TMs contained sign...

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Publication status:
Published

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Publisher copy:
10.1021/bi060355g

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Journal:
Biochemistry
Volume:
45
Issue:
26
Pages:
8088-8095
Publication date:
2006-07-01
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
Source identifiers:
100622
Language:
English
Keywords:
Pubs id:
pubs:100622
UUID:
uuid:1b293db9-1c40-41a5-9919-86dc6105f027
Local pid:
pubs:100622
Deposit date:
2012-12-19

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