1vqe: Difference between revisions
New page: left|200px<br /><applet load="1vqe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vqe, resolution 1.8Å" /> '''GENE V PROTEIN MUTANT... |
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[[Image:1vqe.jpg|left|200px]]<br /><applet load="1vqe" size=" | [[Image:1vqe.jpg|left|200px]]<br /><applet load="1vqe" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1vqe, resolution 1.8Å" /> | caption="1vqe, resolution 1.8Å" /> | ||
'''GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 AND ILE 47 REPLACED BY MET 47 (V35I, I47M)'''<br /> | '''GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 AND ILE 47 REPLACED BY MET 47 (V35I, I47M)'''<br /> | ||
==Overview== | ==Overview== | ||
The problem of rationally engineering protein molecules can be simplified | The problem of rationally engineering protein molecules can be simplified where effects of mutations on protein function are additive. Crystal structures of single and double mutants in the hydrophobic core of gene V protein indicate that structural and functional effects of core mutations are additive when the regions structurally influenced by the mutations do not substantially overlap. These regions of influence can provide a simple basis for identifying sets of mutations that will show additive effects. | ||
==About this Structure== | ==About this Structure== | ||
1VQE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_f1 Bacteriophage f1]. Full crystallographic information is available from [http:// | 1VQE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_f1 Bacteriophage f1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VQE OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Bacteriophage f1]] | [[Category: Bacteriophage f1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Skinner, M | [[Category: Skinner, M M.]] | ||
[[Category: Terwilliger, T | [[Category: Terwilliger, T C.]] | ||
[[Category: dna-binding protein]] | [[Category: dna-binding protein]] | ||
[[Category: gene v]] | [[Category: gene v]] | ||
[[Category: mutant]] | [[Category: mutant]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:37:31 2008'' |
Revision as of 16:37, 21 February 2008
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GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ILE 35 AND ILE 47 REPLACED BY MET 47 (V35I, I47M)
OverviewOverview
The problem of rationally engineering protein molecules can be simplified where effects of mutations on protein function are additive. Crystal structures of single and double mutants in the hydrophobic core of gene V protein indicate that structural and functional effects of core mutations are additive when the regions structurally influenced by the mutations do not substantially overlap. These regions of influence can provide a simple basis for identifying sets of mutations that will show additive effects.
About this StructureAbout this Structure
1VQE is a Single protein structure of sequence from Bacteriophage f1. Full crystallographic information is available from OCA.
ReferenceReference
Potential use of additivity of mutational effects in simplifying protein engineering., Skinner MM, Terwilliger TC, Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10753-7. PMID:8855252
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