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Revision as of 17:26, 25 July 2012
CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V121A MUTANTCONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V121A MUTANT
Template:ABSTRACT PUBMED 9020766
About this StructureAbout this Structure
1oud is a 1 chain structure of Hen Egg-White (HEW) Lysozyme with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ 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