Hydrolysis of chemically distinct sites of human serum albumin by polyoxometalate: A hybrid QM/MM (ONIOM) study.
QM/MM (ONIOM) method
human serum albumin
peptide hydrolysis
polyoxometalates
reaction mechanism
Journal
Journal of computational chemistry
ISSN: 1096-987X
Titre abrégé: J Comput Chem
Pays: United States
ID NLM: 9878362
Informations de publication
Date de publication:
05 01 2019
05 01 2019
Historique:
received:
28
05
2018
revised:
22
06
2018
accepted:
23
06
2018
pubmed:
22
9
2018
medline:
2
6
2020
entrez:
22
9
2018
Statut:
ppublish
Résumé
In this study, mechanisms of hydrolysis of all four chemically diverse cleavage sites of human serum albumin (HSA) by [Zr(OH)(PW
Substances chimiques
Tungsten Compounds
0
polyoxometalate I
0
Serum Albumin, Human
ZIF514RVZR
Types de publication
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
51-61Informations de copyright
© 2018 Wiley Periodicals, Inc.