Literature DB >> 2223774

Sequential assignment of the 1H nuclear magnetic resonance spectrum of barnase.

M Bycroft1, R N Sheppard, F T Lau, A R Fersht.   

Abstract

Two-dimensional nuclear magnetic resonance spectroscopy has been used to study the bacterial ribonuclease barnase (MW 12,382). Resonance assignments have been made for protons in all of the 110 residues. Analysis of medium- and long-range contacts in NOESY spectra has demonstrated that the major elements of secondary structure in barnase in solution are essentially identical with those found in the crystal structure.

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Year:  1990        PMID: 2223774     DOI: 10.1021/bi00484a011

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  5 in total

1.  Positive theta-angles in proteins by nuclear magnetic resonance spectroscopy.

Authors:  S Ludvigsen; F M Poulsen
Journal:  J Biomol NMR       Date:  1992-05       Impact factor: 2.835

2.  Protein simulations: the absorption spectrum of barnase point mutants.

Authors:  Ken R F Somers; Peter Krüger; Sylwia Bucikiewicz; Marc De Maeyer; Yves Engelborghs; Arnout Ceulemans
Journal:  Protein Sci       Date:  2004-07       Impact factor: 6.725

3.  Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways.

Authors:  J Clarke; A M Hounslow; M Bycroft; A R Fersht
Journal:  Proc Natl Acad Sci U S A       Date:  1993-11-01       Impact factor: 11.205

4.  Toward solving the folding pathway of barnase: the complete backbone 13C, 15N, and 1H NMR assignments of its pH-denatured state.

Authors:  V L Arcus; S Vuilleumier; S M Freund; M Bycroft; A R Fersht
Journal:  Proc Natl Acad Sci U S A       Date:  1994-09-27       Impact factor: 11.205

5.  Refolding of barnase mutants and pro-barnase in the presence and absence of GroEL.

Authors:  T E Gray; J Eder; M Bycroft; A G Day; A R Fersht
Journal:  EMBO J       Date:  1993-11       Impact factor: 11.598

  5 in total

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