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2onq

From Proteopedia

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{{STRUCTURE_2onq| PDB=2onq | SCENE= }}
{{STRUCTURE_2onq| PDB=2onq | SCENE= }}
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'''Gbeta1 stabilization by in vitro evolution and computational design'''
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===Gbeta1 stabilization by in vitro evolution and computational design===
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==Overview==
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Computational design and in vitro evolution are major strategies for stabilizing proteins. For the four critical positions 16, 18, 25, and 29 of the B domain of the streptococcal protein G (Gbeta1), they identified the same optimal residues at positions 16 and 25, but not at 18 and 29. Here we analyzed the energetic contributions of the residues from these two approaches by single and double mutant analyses and determined crystal structures for a variant from the calculation (I16/L18/E25/K29) and from the selection (I16/I18/E25/F29). The structural analysis explains the observed differences in stabilization. Residues 16, 18, and 29 line an invagination, which results from a packing defect between the helix and the beta-sheet of Gbeta1. In all stabilized variants, residues with larger side-chains occur at these positions and packing is improved. In the selected variant, packing is better optimized than in the computed variant. Such differences in side-chain packing strongly affect stability but are difficult to evaluate by computation.
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(as it appears on PubMed at http://www.pubmed.gov), where 17868696 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17868696}}
==About this Structure==
==About this Structure==
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[[Category: Improved hydrophobic packing of core residue]]
[[Category: Improved hydrophobic packing of core residue]]
[[Category: Protein binding]]
[[Category: Protein binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:17:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 6 00:59:00 2008''

Revision as of 21:59, 5 July 2008

Image:2onq.png

Template:STRUCTURE 2onq

Gbeta1 stabilization by in vitro evolution and computational design

Template:ABSTRACT PUBMED 17868696

About this Structure

2ONQ is a Single protein structure of sequence from Streptococcus sp.. Full crystallographic information is available from OCA.

Reference

Optimization of the gbeta1 domain by computational design and by in vitro evolution: structural and energetic basis of stabilization., Wunderlich M, Max KE, Roske Y, Mueller U, Heinemann U, Schmid FX, J Mol Biol. 2007 Oct 26;373(3):775-84. Epub 2007 Aug 19. PMID:17868696

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