Molecular interactions in protein crystals: Solvent accessible surface and stability
- 1 January 1990
- journal article
- research article
- Published by Wiley in Proteins-Structure Function and Bioinformatics
- Vol. 8 (1) , 1-5
- https://doi.org/10.1002/prot.340080103
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.Keywords
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