### Abstract

Original language | English |
---|---|

Pages (from-to) | 5706-5717 |

Number of pages | 12 |

Journal | Journal of Chemical Theory and Computation |

Volume | 9 |

Issue number | 12 |

Early online date | 9 Oct 2013 |

DOIs | |

Publication status | Published - 10 Dec 2013 |

### Fingerprint

### Keywords

- bovine chymosin
- bovine milk
- molecular integral equation theory
- solvent binding analysis
- computational alanine scanning
- bovine chymosin-bovine κ-casein complex

### Cite this

*Journal of Chemical Theory and Computation*,

*9*(12), 5706-5717. https://doi.org/10.1021/ct400605x

}

*Journal of Chemical Theory and Computation*, vol. 9, no. 12, pp. 5706-5717. https://doi.org/10.1021/ct400605x

**Solvent binding analysis and computational alanine scanning of the bovine chymosin-bovine κ-casein complex using molecular integral equation theory.** / Palmer, David; Sørensen, Jesper Givskov J.G.; Schiøtt, Birgit B.; Fedorov, Maxim V. M.V.

Research output: Contribution to journal › Article

TY - JOUR

T1 - Solvent binding analysis and computational alanine scanning of the bovine chymosin-bovine κ-casein complex using molecular integral equation theory

AU - Palmer, David

AU - Sørensen, Jesper Givskov J.G.

AU - Schiøtt, Birgit B.

AU - Fedorov, Maxim V. M.V.

PY - 2013/12/10

Y1 - 2013/12/10

N2 - We demonstrate that the relative binding thermodynamics of single-point mutants of a model protein-peptide complex (the bovine chymosin-bovine κ-casein complex) can be calculated accurately and efficiently using molecular integral equation theory. The results are shown to be in good overall agreement with those obtained using implicit continuum solvation models. Unlike the implicit continuum models, however, molecular integral equation theory provides useful information about the distribution of solvent density. We find that experimentally observed water-binding sites on the surface of bovine chymosin can be identified quickly and accurately from the density distribution functions computed by molecular integral equation theory. The bovine chymosin-bovine κ-casein complex is of industrial interest because bovine chymosin is widely used to cleave bovine κ-casein and to initiate milk clotting in the manufacturing of processed dairy products. The results are interpreted in light of the recent discovery that camel chymosin is a more efficient clotting agent than bovine chymosin for bovine milk.

AB - We demonstrate that the relative binding thermodynamics of single-point mutants of a model protein-peptide complex (the bovine chymosin-bovine κ-casein complex) can be calculated accurately and efficiently using molecular integral equation theory. The results are shown to be in good overall agreement with those obtained using implicit continuum solvation models. Unlike the implicit continuum models, however, molecular integral equation theory provides useful information about the distribution of solvent density. We find that experimentally observed water-binding sites on the surface of bovine chymosin can be identified quickly and accurately from the density distribution functions computed by molecular integral equation theory. The bovine chymosin-bovine κ-casein complex is of industrial interest because bovine chymosin is widely used to cleave bovine κ-casein and to initiate milk clotting in the manufacturing of processed dairy products. The results are interpreted in light of the recent discovery that camel chymosin is a more efficient clotting agent than bovine chymosin for bovine milk.

KW - bovine chymosin

KW - bovine milk

KW - molecular integral equation theory

KW - solvent binding analysis

KW - computational alanine scanning

KW - bovine chymosin-bovine κ-casein complex

UR - http://www.scopus.com/inward/record.url?scp=84890497066&partnerID=8YFLogxK

U2 - 10.1021/ct400605x

DO - 10.1021/ct400605x

M3 - Article

AN - SCOPUS:84890497066

VL - 9

SP - 5706

EP - 5717

JO - Journal of Chemical Theory and Computation

JF - Journal of Chemical Theory and Computation

SN - 1549-9618

IS - 12

ER -