Journal
PROTEIN SCIENCE
Volume 9, Issue 7, Pages 1391-1394Publisher
CAMBRIDGE UNIV PRESS
DOI: 10.1110/ps.9.7.1391
Keywords
helix dipole interaction; helix propensity; protein design; protein G
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Six helix surface positions of protein G (G beta 1) were redesigned using a computational protein design algorithm, resulting in the five fold mutant G beta 1m2. G beta 1m2 is well folded with a circular dichroism spectrum nearly identical to that of G beta 1, and a melting temperature of 91 degrees C, similar to 6 degrees C higher than that of G beta 1. The crystal structure of G beta 1m2 was solved to 2.0 Angstrom resolution by molecular replacement. The absence of hydrogen bond or salt bridge interactions between the designed residues in G beta 1m2 suggests that the increased stability of G beta 1m2 is due to increased helix propensity and more favorable helix dipole interactions.
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