Article
Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design.
Protein science : a publication of the Protein Society - 1 Jul 2000
Strop P, Marinescu A M, Mayo S L
Abstract excerpt
Six helix surface positions of protein G (Gbeta1) were redesigned using a computational protein design algorithm, resulting in the five fold mutant Gbeta1m2. Gbeta1m2 is well folded with a circular dichroism spectrum nearly identical to that of Gbeta1, and a melting temperature of 91 degrees C, approximately 6 degrees C higher than that of Gbeta1. The crystal structure of Gbeta1m2 was solved to 2.0 A resolution...
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