Hot-Spot Mapping of the Interactions between Chymosin and Bovine κ-Casein-Reference-Cited by-同舟云学术

Hot-Spot Mapping of the Interactions between Chymosin and Bovine κ-Casein

Published:2013-08-07 Issue:33 Volume:61 Page:7949-7959
ISSN:0021-8561
Container-title:Journal of Agricultural and Food Chemistry
language:en
Short-container-title:J. Agric. Food Chem.

Author:

Sørensen Jesper¹,Palmer David S.¹,Schiøtt Birgit¹

Affiliation:

1. The Center for Insoluble Protein Structures (inSPIN) and the Interdisciplinary Nanoscience Center (iNANO) and ‡Department of Chemistry, Aarhus University, Langelandsgade 140, DK-8000 Aarhus C, Denmark

Publisher

American Chemical Society (ACS)

Subject

General Agricultural and Biological Sciences,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jf4021043

Reference59 articles.

1. The Production, Action and Application of Rennet and Coagulants

2. The primary structure of calf chymosin.

3. Post X-ray crystallographic studies of chymosin: the existence of two structural forms and the regulation of activity by the interaction with the histidine-proline cluster of κ-casein

4. Characterization of recombinant camel chymosin reveals superior properties for the coagulation of bovine and camel milk

5. Clustal W and Clustal X version 2.0

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