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1brh

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[[Image:1brh.png|left|200px]]
[[Image:1brh.png|left|200px]]
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{{STRUCTURE_1brh| PDB=1brh | SCENE= }}
{{STRUCTURE_1brh| PDB=1brh | SCENE= }}
===BARNASE MUTANT WITH LEU 14 REPLACED BY ALA===
===BARNASE MUTANT WITH LEU 14 REPLACED BY ALA===
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{{ABSTRACT_PUBMED_8605178}}
{{ABSTRACT_PUBMED_8605178}}
==About this Structure==
==About this Structure==
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1BRH is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BRH OCA].
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[[1brh]] is a 3 chain structure of [[Barnase]] and [[Ribonuclease]] with sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BRH OCA].
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==See Also==
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*[[Barnase|Barnase]]
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*[[Ribonuclease|Ribonuclease]]
==Reference==
==Reference==
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<ref group="xtra">PMID:8605178</ref><references group="xtra"/>
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<ref group="xtra">PMID:008605178</ref><references group="xtra"/>
[[Category: Bacillus amyloliquefaciens]]
[[Category: Bacillus amyloliquefaciens]]
[[Category: Buckle, A.]]
[[Category: Buckle, A.]]
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[[Category: Fersht, A.]]
[[Category: Fersht, A.]]
[[Category: Alpha/beta protein]]
[[Category: Alpha/beta protein]]
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[[Category: Endonuclease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 14:18:30 2009''
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Revision as of 14:31, 25 July 2012

Template:STRUCTURE 1brh

Contents

BARNASE MUTANT WITH LEU 14 REPLACED BY ALA

Template:ABSTRACT PUBMED 8605178

About this Structure

1brh is a 3 chain structure of Barnase and Ribonuclease with sequence from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA.

See Also

Reference

  • Buckle AM, Cramer P, Fersht AR. Structural and energetic responses to cavity-creating mutations in hydrophobic cores: observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities. Biochemistry. 1996 Apr 9;35(14):4298-305. PMID:8605178 doi:http://dx.doi.org/10.1021/bi9524676

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