Literature DB >> 14269311

THERMODYNAMICS OF CONFORMATIONAL CHANGES OF PROTEINS. I. PH-DEPENDENT DENATURATION OF MURAMIDASE.

A J SOPHIANOPOULOS, B J WEISS.   

Abstract

Keywords:  CHEMISTRY; EXPERIMENTAL LAB STUDY; HYDROGEN-ION CONCENTRATION; MURAMIDASE; PROTEIN DENATURATION; TEMPERATURE; THERMODYNAMICS; VISCOSITY

Mesh：

Substances：

Year:  1964        PMID： 14269311     DOI： 10.1021/bi00900a023

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


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  6 in total

1.  A possible origin of differences between calorimetric and equilibrium estimates of stability parameters of proteins.

Authors:  A Sinha; S Yadav; R Ahmad; F Ahmad
Journal:  Biochem J       Date:  2000-02-01       Impact factor: 3.857

2.  Highly perturbed pKa values in the unfolded state of hen egg white lysozyme.

Authors:  John Bradley; Fergal O'Meara; Damien Farrell; Jens Erik Nielsen
Journal:  Biophys J       Date:  2012-04-03       Impact factor: 4.033

Review 3.  The problem of the stability globular proteins.

Authors:  W Pfeil
Journal:  Mol Cell Biochem       Date:  1981-10-09       Impact factor: 3.396

4.  Spectroscopic, immunochemical, and thermodynamic properties of carboxymethyl(Cys6, Cys127)-hen egg white lysozyme.

Authors:  M E Denton; H A Scheraga
Journal:  J Protein Chem       Date:  1991-04

5.  Effects of pH and temperature on the wild-type and a mutant form of Neurospora glutamate dehydrogenase.

Authors:  J R Fincham; H R Garner
Journal:  Biochem J       Date:  1967-06       Impact factor: 3.857

6.  Detection of new temperature-dependent conformational transition in lysozyme by carbon-13 nuclear magnetic resonance spectroscopy.

Authors:  P J Cozzone; S J Opella; O Jardetzky; J Berthou; P Jollès
Journal:  Proc Natl Acad Sci U S A       Date:  1975-06       Impact factor: 11.205
  6 in total

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