On the effect of mutations in bovine or camel chymosin on the thermodynamics of binding κ-caseins-Reference-Cited by-同舟云学术

On the effect of mutations in bovine or camel chymosin on the thermodynamics of binding κ-caseins

Published:2017-11-08 Issue:1 Volume:86 Page:75-87
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Ansari Samiul M.¹,Sørensen Jesper²,Schiøtt Birgit²,Palmer David S.¹^ORCID

Affiliation:

1. Department of Pure and Applied Chemistry; University of Strathclyde, Thomas Graham Building, 295 Cathedral Street; Glasgow G1 1XL Scotland

2. Interdisciplinary Nanoscience Center (iNANO) and Department of Chemistry; University of Aarhus, Langelandsgade 140; Aarhus DK 8000 Denmark

Funder

Engineering and Physical Sciences Research Council

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/prot.25410/fullpdf

Reference76 articles.

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2. Characterization of recombinant camel chymosin reveals superior properties for the coagulation of bovine and camel milk;Kappeler;Biochem Biophys Res Commun.,2006

3. Bovine Chymosin: A Computational Study of Recognition and Binding of Bovine κ-Casein;Palmer;Biochemistry.,2010

4. The active site of aspartic proteinases;Pearl;FEBS Lett.,1984

5. X-ray analyses of aspartic proteinase: V structure and refinement at 2.0A resolution of the aspartic proteinase from Mucor pusillus;Newman;J Mol Biol.,1993

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