Literature DB >> 4361856

NMR relaxation studies of the unfolding and refolding of staphylococcal nuclease at low pH.

Y Arata, R Khalifah, O Jardetzky.   

Abstract

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Year:  1973        PMID： 4361856     DOI： 10.1111/j.1749-6632.1973.tb15265.x

Source DB:  PubMed          Journal:  Ann N Y Acad Sci        ISSN： 0077-8923            Impact factor:   5.691


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  3 in total

1.  Predicting extreme pKa shifts in staphylococcal nuclease mutants with constant pH molecular dynamics.

Authors:  Evan J Arthur; Joseph D Yesselman; Charles L Brooks
Journal:  Proteins       Date:  2011-10-15

Review 2.  Staphylococcal nuclease reviewed: a prototypic study in contemporary enzymology. IV. The nuclease as a model for protein folding.

Authors:  P W Tucker; E E Hazen; F A Cotton
Journal:  Mol Cell Biochem       Date:  1979-02-09       Impact factor: 3.396

3.  Proton longitudinal relaxation investigation of histidyl residues in human normal adult hemoglobin.

Authors:  I M Russu; C Ho
Journal:  Biophys J       Date:  1982-08       Impact factor: 4.033
  3 in total

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