1gb4: Difference between revisions

Revision as of 05:01, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1gb4.png

Template:STRUCTURE 1gb4

HYPERTHERMOPHILIC VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G, NMR, 47 STRUCTURESHYPERTHERMOPHILIC VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G, NMR, 47 STRUCTURES

Template:ABSTRACT PUBMED 9628485

About this StructureAbout this Structure

1GB4 is a Single protein structure of sequence from Streptococcus sp.. Full experimental information is available from OCA.

ReferenceReference

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''HYPERTHERMOPHILIC VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G, NMR, 47 STRUCTURES'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9628485}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9628485 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9628485}}
 ==About this Structure==
-GB4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_sp. Streptococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GB4 OCA].
+GB4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_sp. Streptococcus sp.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GB4 OCA].
 ==Reference==
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 [[Category: Hyperthermophile]]
 [[Category: Streptococcal protein g]]
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