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Title
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Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles.
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Authors
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H.Nicholson,
W.J.Becktel,
B.W.Matthews.
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Ref.
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Nature, 1988,
336,
651-656.
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PubMed id
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Abstract
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Two different genetically engineered amino-acid substitutions designed to
interact with alpha-helix dipoles in T4 lysozyme are shown to increase the
thermal stability of the protein. Crystallographic analyses of the mutant
lysozyme structures suggest that the stabilization is due to electrostatic
interaction and does not require precise hydrogen bonding between the
substituted amino acid and the end of the alpha-helix.
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