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The optimization of protein-solvent interactions: thermostability and the role of hydrophobic and electrostatic interactions.

Protein-solvent interactions were analyzed using an optimization parameter based on the ratio of the solvent-accessible area in the native and the unfolded protein structure. The calculations were performed for a set of 183 nonhomologous proteins with known three-dimensional structure available in t...

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Bibliografiske detaljer
Main Authors: Spassov, V. Z., Karshikoff, A. D., Ladenstein, R.
Format: Artigo
Sprog:Inglês
Udgivet: Cold Spring Harbor Laboratory Press 1995
Fag:
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC2143201/
https://ncbi.nlm.nih.gov/pubmed/8520477
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