Article
Paired natural cysteine mutation mapping: aid to constraining models of protein tertiary structure.
Protein science : a publication of the Protein Society - 1 Nov 1995
Kreisberg R, Buchner V, Arad D
Abstract excerpt
This paper discusses the benefit of mapping paired cysteine mutation patterns as a guide to identifying the positions of protein disulfide bonds. This information can facilitate the computer modeling of protein tertiary structure. First, a simple, paired natural-cysteine-mutation map is presented that identifies the positions of putative disulfide bonds in protein families. The method is based on the observation...
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