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Chemicals, plastics and rubber industries

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Molecular dynamics simulations of staphylococcal nuclease: Properties of water at the protein surface

Article Abstract:

A molecular dynamics study of fully hydrated, native staphylococcal nuclease (SNase) is reported. Further, findings of the research conducted for the analysis of the structural properties of the water at the protein surface (density profile, coordination numbers, hydrogen-bond distribution) are presented.

Author: Winter, Roland, Smolin, Nikolai
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2004
Water, Chemical properties

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Sequential collapse folding pathway of staphylococcal nuclease: entropic activation barriers to hydrophobic collapse of the protein core

Article Abstract:

The folding pathway of staphylococcal nuclease is revealed with the help of the sequential collapse model (SCM). The SCM suggests that the observed activation barriers have a configurational entropic origin related to the hydrophobic collapse process of the three predicted parallel folding pathways.

Author: Bergasa-Caceres, Fernando, Rabitz, Herschel A.
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2004
Hydrophobic effect

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Sequential collapse model for protein folding pathways

Article Abstract:

Issues concerning the determination of the sequence of events along the folding pathway of globular proteins of limited size at low resolution are discussed. The sequential collapse model offers a simple structure for explaining protein folding pathways.

Author: Bergasa-Caceres, Fernando, Rabitz, Herschel A., Ronneberg, T. Andrew
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 1999
Models, Protein folding

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Subjects list: Research, Staphylococcus, Nucleases
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