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Structure of a methionine‐rich segment of Escherichia coli Ffh protein
Author(s) -
Oh Doo-Byoung,
Yi Gwan-Su,
Chi Seung-Wook,
Kim Hyoungman
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)01019-8
Subject(s) - methionine , escherichia coli , peptide , chemistry , alpha helix , helix (gastropod) , aqueous solution , residue (chemistry) , crystallography , protein structure , amphiphile , biochemistry , amino acid , biophysics , biology , organic chemistry , gene , ecology , snail , copolymer , polymer
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 α‐helix conformation exists even in water and this peptide assumes a stable α‐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 α‐helical structure.