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1em7

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{{STRUCTURE_1em7| PDB=1em7 | SCENE= }}
{{STRUCTURE_1em7| PDB=1em7 | SCENE= }}
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'''HELIX VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G'''
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===HELIX VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G===
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==Overview==
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Six helix surface positions of protein G (Gbeta1) were redesigned using a computational protein design algorithm, resulting in the five fold mutant Gbeta1m2. Gbeta1m2 is well folded with a circular dichroism spectrum nearly identical to that of Gbeta1, and a melting temperature of 91 degrees C, approximately 6 degrees C higher than that of Gbeta1. The crystal structure of Gbeta1m2 was solved to 2.0 A resolution by molecular replacement. The absence of hydrogen bond or salt bridge interactions between the designed residues in Gbeta1m2 suggests that the increased stability of Gbeta1m2 is due to increased helix propensity and more favorable helix dipole interactions.
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(as it appears on PubMed at http://www.pubmed.gov), where 10933505 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10933505}}
==About this Structure==
==About this Structure==
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[[Category: Protein design]]
[[Category: Protein design]]
[[Category: Protein g]]
[[Category: Protein g]]
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Revision as of 21:58, 30 June 2008

Image:1em7.png

Template:STRUCTURE 1em7

HELIX VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G

Template:ABSTRACT PUBMED 10933505

About this Structure

1EM7 is a Single protein structure of sequence from Streptococcus sp.. Full crystallographic information is available from OCA.

Reference

Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design., Strop P, Marinescu AM, Mayo SL, Protein Sci. 2000 Jul;9(7):1391-4. PMID:10933505

Page seeded by OCA on Tue Jul 1 00:58:18 2008

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