Surface dynamics of the integral membrane protein bacteriorhodopsin
Surface dynamics of the integral membrane protein bacteriorhodopsin
复制标题
整合膜蛋白细菌视紫红质的表面动力学
作者:
M. Keniry;H. S. Gutowsky;E. Oldfield
Recently, there has been great interest in determining the three-dimensional structures of membrane proteins, particularly bacteriorhodopsin, for which a variety of possible folding arrangements have been suggested1–4. In this paper we present nuclear magnetic resonance (NMR) spectra5–8 of deuterated bacteriorhodopsin, and use the data to help interpret the various suggested bacteriorhodopsin folding patterns. The results strongly indicate that (1) a membrane surface (±1 residue) may be defined by NMR in bacteriorhodopsin; (2) all amino acids inside the surface are essentially crystalline; (3) all amino acids outside the surface (surface residues) in bacteriorhodopsin are highly mobile on the time scale of the 2H NMR experiments; (4) NMR data may be used to help evaluate the various structural models that have been proposed; (5) aggregation of purple membrane sheets may lead to an immobilization of the surface residues.
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DOI:
--
发表时间:
1981
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Kinsey,RA;Kintanar,A;Oldfield,E
通讯作者:
Oldfield,E
DOI:
10.1016/s0021-9258(19)69982-5
发表时间:
1981-02
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
T. Rothgeb;E. Oldfield
通讯作者:
T. Rothgeb;E. Oldfield
DOI:
--
发表时间:
1982
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Huang,KS;Radhakrishnan,R;Bayley,H;Khorana,HG
通讯作者:
Khorana,HG
DOI:
--
发表时间:
1981
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Kinsey,RA;Kintanar,A;Tsai,MD;Smith,RL;Janes,N;Oldfield,E
通讯作者:
Oldfield,E