Journal article
Solvent accessibility properties of complex proteins
Abstract
AN important factor in the thermodynamics of protein folding is the partition of amino acid residues between the solvent environment and the protein core. The extent of the interaction between the folded polypeptide and the surrounding medium can be measured by determining the solvent accessible surface area as defined by Lee and Richards1. In this communication we present the results of solvent accessibility calculations for the large (195,000 …
Authors
SPRANG S; YANG D; FLETTERICK RJ
Journal
Nature, Vol. 280, No. 5720, pp. 333–335
Publisher
Springer Nature
Publication Date
July 1979
DOI
10.1038/280333a0
ISSN
0028-0836