当前位置： SCI文献检索 > JOURNAL OF BIOMOLECULAR NMR期刊下所有文献 > Estimates of phi and psi torsion angles in proteins from one-, two- and three-bond nuclear spin-spin couplings: application to staphylococcal nuclease.

Estimates of phi and psi torsion angles in proteins from one-, two- and three-bond nuclear spin-spin couplings: application to staphylococcal nuclease.

Abstract：

:Calculated coupling constants (3JHNH alpha, 1JC alpha H alpha, 2JC'H alpha, 1JC alpha N and 2JC alpha N) from our accompanying paper [Edison, A.S. et al. (1994) J. Biomol. NMR, 4, 519-542] have been used to generate error surfaces that can provide estimates of the phi and psi angles in proteins. We have used experimental coupling data [3JHNH alpha: Kay, L.E. et al. (1989) J. Am. Chem. Soc., 111, 5488-5490; 1JC alpha H alpha: Vuister, G. W. et al. (1993) J. Biomol. NMR, 3, 67-80; 2JC'H alpha: Vuister, G.W. and Bax, A. (1992) J. Biomol. NMR, 2, 401-405; 1JC alpha N and 2JC alpha N: Delaglio, F. et al. (1991) J. Biomol. NMR, 1, 439-446] to create error surfaces for selected residues of the protein staphylococcal nuclease. The residues were chosen to include all those with five experimental couplings, as well as some with four experimental couplings, to demonstrate the relative importance of 3JHNH alpha and 1JC alpha H alpha. For most of the cases, we obtained good agreement between the X-ray structure [Loll, P.J. and Lattman, E.E. (1989) Protein Struct. Funct. Genet., 5, 183-201] and the NMR data.

journal_name

J Biomol NMR

journal_title

Journal of biomolecular NMR

authors

Edison AS,Weinhold F,Westler WM,Markley JL

doi

10.1007/BF00156619

subject

Has Abstract

pub_date

1994-07-01 00:00:00

pages

543-51

issue

4

eissn

0925-2738

issn

1573-5001

journal_volume

4

pub_type

杂志文章

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