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Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design
Author(s) -
Strop Pavel,
Marinescu Andrei M.,
Mayo Stephen L.
Publication year - 2000
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.9.7.1391
Subject(s) - helix (gastropod) , circular dichroism , crystallography , hydrogen bond , chemistry , protein structure , dipole , alpha helix , molecule , biology , biochemistry , ecology , organic chemistry , snail
Six helix surface positions of protein G (Gβ1) were redesigned using a computational protein design algorithm, resulting in the five fold mutant Gβ1m 2 . Gβ1m 2 is well folded with a circular dichroism spectrum nearly identical to that of Gβ1, and a melting temperature of 91 °C, ∼6°C higher than that of Gβ1. The crystal structure of Gβ1m 2 was solved to 2.0 Å resolution by molecular replacement. The absence of hydrogen bond or salt bridge interactions between the designed residues in Gβ1m 2 suggests that the increased stability of Gβ1m 2 is due to increased helix propensity and more favorable helix dipole interactions.