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Journal article

Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions.

Abstract:

Membrane model systems consisting of phosphatidylcholines and hydrophobic alpha-helical peptides with tryptophan flanking residues, a characteristic motif for transmembrane protein segments, were used to investigate the contribution of tryptophans to peptide-lipid interactions. Peptides of different lengths and with the flanking tryptophans at different positions in the sequence were incorporated in relatively thick or thin lipid bilayers. The organization of the systems was assessed by NMR m...

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Publication status:
Published

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Publisher copy:
10.1021/bi027000r

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Journal:
Biochemistry
Volume:
42
Issue:
18
Pages:
5341-5348
Publication date:
2003-05-01
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
Source identifiers:
100691
Language:
English
Keywords:
Pubs id:
pubs:100691
UUID:
uuid:5108045c-e610-46b4-a096-30030127c6cb
Local pid:
pubs:100691
Deposit date:
2012-12-19

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