PMID:8898086
| Citation |
Oh, DB, Yi, GS, Chi, SW and Kim, H (1996) Structure of a methionine-rich segment of Escherichia coli Ffh protein. FEBS Lett. 395:160-4 |
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| Abstract |
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. |
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| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Circular Dichroism; Escherichia coli; Escherichia coli Proteins; Magnetic Resonance Spectroscopy; Methionine; Molecular Sequence Data; Peptide Fragments/chemical synthesis; Peptide Fragments/chemistry; Protein Conformation; Signal Recognition Particle/chemistry |
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