Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy-Reference-Cited by-同舟云学术

Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy

Published:1995-12 Issue:12 Volume:4 Page:2605-2615
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Sci.

Author:

Frank M. Kirsten,Clore G. Marius,Gronenborn Angela M.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference56 articles.

1. 1.67-Å X-ray structure of the B2 immunoglobulin-binding domain of streptococcal protein G and comparison to the NMR structure of the Bl domain;Achari;Biochemistry,1992

2. Effects of ion binding on the backbone dynamics of calbinin determined by 15N NMR relaxation;Akke;Biochemistry,1993

3. Kinetic analysis of folding and unfolding of the 56 amino acid IgG-binding domain of streptococcal protein G;Alexander;Biochemistry,1992

4. Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: A heteronuclear NMR study;Alexandrescu;Biochemistry,1994

5. Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: A two-dimensional NMR study;Alexandrescu;Biochemistry,1993

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