Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design

Six helix surface positions of protein G (Gβ1) were redesigned using a computational protein design algorithm, resulting in the five fold mutant Gβ1m2. Gβ1m2 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...

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Veröffentlicht in:	Protein science 2000-07, Vol.9 (7), p.1391-1394
Hauptverfasser:	STROP, PAVEL, MARINESCU, ANDREI M., MAYO, STEPHEN L.
Format:	Artikel
Sprache:	eng
Schlagworte:	Algorithms Crystallography, X-Ray FOR THE RECORD helix dipole interaction helix propensity Hydrogen Bonding Models, Molecular Mutation Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - genetics Protein Conformation protein design Protein Engineering - methods protein G Static Electricity
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