Proceedings of the Korean Biophysical Society Conference (한국생물물리학회:학술대회논문집)
- 1996.07a
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- Pages.26-26
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- 1996
Structure of a Methionine-Rich Segment of Escherichia coli Fifty Four Homologue Protein
- Oh, Doo-Byoung (Department of Biological Sciences, Korea Advanced Institute of Science and Technology) ;
- Yi, Gwan-Su (Magnetic Resonance Group, Korea Basic Science Institut) ;
- Chi, Seung-Wook (Department of Biological Sciences, Korea Advanced Institute of Science and Technolog) ;
- Kim, Hyoungman (Department of Biological Sciences, Korea Advanced Institute of Science and Technology)
- Published : 1996.07.01
Abstract
The methionine-rich segments of the Fifty four homologue (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 ard NMR. (omitted)
Keywords