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

FEBS Letters

Yi, Gwan-Su²  Kim, Hyoungman¹  Oh, Doo-Byoung¹  Chi, Seung-Wook¹ 

[1] Department of Biological Sciences, Korea Advanced Institute of Science and Technology, 373-1 Kusong-Dong, Yusong-Gu, Taejon 305-701, South Korea;Magnetic Resonance Group, Korea Basic Science Institute, Taejon 305-333, South Korea

关键词: Ffh protein;    Peptide;    NMR;    CD;    α-Helix;    Translocation;    Ffh;    fifty-four homologue;    SRP;    signal recognition particle;    SRP54;    54 kDa subunit of signal recognition particle;    CD;    circular dichroism;    TFE;    2;    2;    2-trifluroethanol;   

DOI  :  10.1016/0014-5793(96)01019-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown