Proposed mechanism for stability of proteins to evolutionary mutations.

doi:10.1073/pnas.95.18.10682

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Article

Proposed mechanism for stability of proteins to evolutionary mutations.

Proceedings of the National Academy of Sciences of the United States of America - 1 Sept 1998

Nelson E D, Onuchic J N

Abstract excerpt

It is shown that the sequence-ordering tendencies induced by design into different fast-folding, thermally stable native structures interfere. This interference results in a type of quasiorthogonality between optimal native structures, which divides sequence space into fast-folding, thermally sta...

Topics

Evolution, Molecular
Hydrogen Bonding
Models, Chemical
Mutation
Protein Folding
Proteins

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