1ouc

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{{STRUCTURE_1ouc| PDB=1ouc | SCENE= }}
{{STRUCTURE_1ouc| PDB=1ouc | SCENE= }}
===CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V110A MUTANT===
===CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V110A MUTANT===
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==About this Structure==
==About this Structure==
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1OUC is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OUC OCA].
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[[1ouc]] is a 1 chain structure of [[Hen Egg-White (HEW) Lysozyme]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OUC OCA].
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==See Also==
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*[[Hen Egg-White (HEW) Lysozyme|Hen Egg-White (HEW) Lysozyme]]
==Reference==
==Reference==
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<ref group="xtra">PMID:9020766</ref><references group="xtra"/>
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<ref group="xtra">PMID:009020766</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
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[[Category: Amyloid]]
[[Category: Amyloid]]
[[Category: Disease mutation]]
[[Category: Disease mutation]]
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[[Category: Signal]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 18:28:44 2009''
 

Revision as of 20:39, 25 July 2012

Template:STRUCTURE 1ouc

Contents

CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V110A MUTANT

Template:ABSTRACT PUBMED 9020766

About this Structure

1ouc is a 1 chain structure of Hen Egg-White (HEW) Lysozyme with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Takano K, Yamagata Y, Fujii S, Yutani K. Contribution of the hydrophobic effect to the stability of human lysozyme: calorimetric studies and X-ray structural analyses of the nine valine to alanine mutants. Biochemistry. 1997 Jan 28;36(4):688-98. PMID:9020766 doi:10.1021/bi9621829

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