Structure of a methionine-rich segment of Escherichia coli Ffh protein

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The methionine-rich segments of the Ffh protein of Escherichia coli and its eukaryotic counterpart SRP54 are thought to bind signal sequences of secretory proteins. The structure of a chemically synthesized 25-residue-long peptide corresponding to one of the proposed methionine-rich amphiphilic helices of Ffh was determined in water and in aqueous trifluroethanol (TFE) solution using CD and NMR. An appreciable alpha-helix conformation exists even in water and this peptide assumes a stable alpha-helix along most of its length in aqueous TFE solution, It is clear that this segment of Ffh protein has a very strong propensity to form alpha-helical structure.
Publisher
ELSEVIER SCIENCE BV
Issue Date
1996-10
Language
English
Article Type
Article
Keywords

SIGNAL-RECOGNITION PARTICLE; SECONDARY STRUCTURE; H-1-NMR SPECTRA; SPECTROSCOPY; SEQUENCES; PEPTIDES; BINDING; TRIFLUOROETHANOL; ASSIGNMENT; PARAMETERS

Citation

FEBS LETTERS, v.395, no.2-3, pp.160 - 164

ISSN
0014-5793
DOI
10.1016/0014-5793(96)01019-8
URI
http://hdl.handle.net/10203/72444
Appears in Collection
BiS-Journal Papers(저널논문)
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