1gb4
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(New page: 200px<br /><applet load="1gb4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gb4" /> '''HYPERTHERMOPHILIC VARIANT OF THE B1 DOMAIN F...)
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Revision as of 13:46, 20 November 2007
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HYPERTHERMOPHILIC VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G, NMR, 47 STRUCTURES
Overview
Here we report the use of an objective computer algorithm in the design of, a hyperstable variant of the Streptococcal protein Gbeta1 domain (Gbeta1)., The designed seven-fold mutant, Gbeta1-c3b4, has a melting temperature in, excess of 100 degrees C and an enhancement in thermodynamic stability of, 4.3 kcal mol(-1) at 50 degrees C over the wild-type protein. Gbeta1-c3b4, maintains the Gbeta1 fold, as determined by nuclear magnetic resonance, spectroscopy, and also retains a significant level of binding to human IgG, in qualitative comparisons with wild type. The basis of the stability, enhancement appears to have multiple components including optimized core, packing, increased burial of hydrophobic surface area, more favorable, helix dipole interactions, and improvement of secondary structure, propensity. The design algorithm is able to model such complex, contributions simultaneously using empirical physical/chemical potential, functions and a combinatorial optimization algorithm based on the dead-end, elimination theorem. Because the design methodology is based on general, principles, there is the potential of applying the methodology to the, stabilization of other unrelated protein folds.
About this Structure
1GB4 is a Single protein structure of sequence from Streptococcus sp.. Full crystallographic information is available from OCA.
Reference
Design, structure and stability of a hyperthermophilic protein variant., Malakauskas SM, Mayo SL, Nat Struct Biol. 1998 Jun;5(6):470-5. PMID:9628485
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