Literature DB >> 9691289

NMR assignments for acid-denatured cold shock protein A.

A T Alexandrescu1, K Rathgeb-Szabo.   

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Year:  1998        PMID： 9691289     DOI： 10.1023/a:1008283925446

Source DB:  PubMed          Journal:  J Biomol NMR        ISSN： 0925-2738            Impact factor:   2.835


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  8 in total

1.  A dynamic bundle of four adjacent hydrophobic segments in the denatured state of staphylococcal nuclease.

Authors:  Y Wang; D Shortle
Journal:  Protein Sci       Date:  1996-09       Impact factor: 6.725

2.  Kinetic and magnetic resonance studies of effects of genetic substitution of a Ca2+-liganding amino acid in staphylococcal nuclease.

Authors:  E H Serpersu; D Shortle; A S Mildvan
Journal:  Biochemistry       Date:  1986-01-14       Impact factor: 3.162

Review 3.  Pulsed field gradient multi-dimensional NMR methods for the study of protein structure and dynamics in solution.

Authors:  L E Kay
Journal:  Prog Biophys Mol Biol       Date:  1995       Impact factor: 3.667

4.  The backbone structure of the major cold-shock protein CS7.4 of Escherichia coli in solution includes extensive beta-sheet structure.

Authors:  S Chatterjee; W Jiang; S D Emerson; M Inouye
Journal:  J Biochem       Date:  1993-11       Impact factor: 3.387

5.  Accretion of structure in staphylococcal nuclease: an 15N NMR relaxation study.

Authors:  A T Alexandrescu; W Jahnke; R Wiltscheck; M J Blommers
Journal:  J Mol Biol       Date:  1996-07-26       Impact factor: 5.469

6.  Solution structure of the anticodon-binding domain of Escherichia coli lysyl-tRNA synthetase and studies of its interaction with tRNA(Lys).

Authors:  S Commans; P Plateau; S Blanquet; F Dardel
Journal:  J Mol Biol       Date:  1995-10-13       Impact factor: 5.469

7.  Crystal structure of CspA, the major cold shock protein of Escherichia coli.

Authors:  H Schindelin; W Jiang; M Inouye; U Heinemann
Journal:  Proc Natl Acad Sci U S A       Date:  1994-05-24       Impact factor: 11.205

8.  OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences.

Authors:  A G Murzin
Journal:  EMBO J       Date:  1993-03       Impact factor: 11.598
  8 in total
  1 in total

1.  Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxide.

Authors:  V A Jaravine; K Rathgeb-Szabo; A T Alexandrescu
Journal:  Protein Sci       Date:  2000-02       Impact factor: 6.725
  1 in total

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