Cold-denatured ensemble of apomyoglobin: implications for the early steps of folding
Article Abstract:
Various spectroscopies were used to study the cold-denatured equine apomyoglobin in aqueous solutions at temperatures between -20 to 98 degrees Centigrade. The cold denaturation of apomyoglobin was found to be different from acid-induced folding in many aspects and can be well described by a cooperative transition below 3 degrees Centigrade. Moreover, an examination of the N-terminal A-peptide fragment of equine apomyoglobin in aqueous and trifluoroethanol solutions revealed that cold denaturation leads to the breakdown of the AGH-hydrophobic interface.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 1998
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Hydrophobic effects on a molecular scale
Article Abstract:
Research was conducted to examine hydrophobic hydration and interactions on a molecular scale and the effects of pressure, temperature and salt concentration on them using a new theoretical approach. The objective is to improve the understanding of the molecular origins of hydrophobic effects. Results confirm that the basic information theory model provides a simple theoretical framework to study many hydrophobic phenomena on a molecular scale since it has already led to a new understanding of the temperature dependence of hydrophobic hydration.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 1998
User Contributions:
Comment about this article or add new information about this topic:
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