In:
European Journal of Biochemistry, Wiley, Vol. 215, No. 3 ( 1993-08), p. 573-585
Abstract:
Che Y is a 129‐residue parallel α/β protein involved in bacterial chemotaxis. We have used this protein as a model to study the folding reaction of parallel α/β proteins. As a first step we carried out the complete assignment of the 1 H and 15 N spectra from Escherichia coli Che Y protein on the basis of two‐dimensional 1 H homonuclear and 1 H‐ 15 N heteronuclear experiments by using sequence‐specific methods. Our assignments differ from the preliminary assignments made by Kar et al. [Kar, L., Matsumura, P. & Johnson, M. E. (1992) Biochem. J. 287 , 521–531] of aromatic residues obtained by comparison of NOEs with short proton–proton distances in the crystal structure of Che Y. The analysis of the extension of the secondary elements, as well as a preliminary calculation of the three‐dimensional structure, indicate that the solution structure is closely coincident with the single crystal structure determined by X‐ray diffraction.
Type of Medium:
Online Resource
ISSN:
0014-2956
,
1432-1033
DOI:
10.1111/ejb.1993.215.issue-3
DOI:
10.1111/j.1432-1033.1993.tb18068.x
Language:
English
Publisher:
Wiley
Publication Date:
1993
detail.hit.zdb_id:
1398347-7
detail.hit.zdb_id:
2172518-4
SSG:
12
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