๐”– Bobbio Scriptorium
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Molecular interactions in protein crystals: Solvent accessible surface and stability

โœ Scribed by Suhail A. Islam; Dr. David L. Weaver

Book ID
105358520
Publisher
John Wiley and Sons
Year
1990
Tongue
English
Weight
402 KB
Volume
8
Category
Article
ISSN
0887-3585

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โœฆ Synopsis

Abstract

The accessible surface areas of 58 monomeric and dimeric proteins, when measured in the crystalline environment, are found to be simply related to molecular weight. The loss of accessible surface when the proteins go from a free to their crystalline environment is well defined, implying that the hydrophobic interaction, which has been found to contribute to protein folding and stability in living systems, also contributes to protein crystal stability.

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