Investigation on the interaction of acid phosphatase with putrescine using docking, simulations methods and multispectroscopic techniques.
Acid Phosphatase
/ chemistry
Algorithms
Binding Sites
Enzyme Activation
Enzyme Stability
Hydrogen Bonding
Hydrogen-Ion Concentration
Hydrophobic and Hydrophilic Interactions
Kinetics
Models, Theoretical
Molecular Docking Simulation
Molecular Dynamics Simulation
Protein Binding
Putrescine
/ chemistry
Spectrum Analysis
Thermodynamics
Circular dichroism (CD)
Kinetic techniques
Molecular dynamics (MD) simulations
Thermal stability
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
01 May 2020
01 May 2020
Historique:
received:
01
11
2019
revised:
04
02
2020
accepted:
06
02
2020
pubmed:
12
2
2020
medline:
29
12
2020
entrez:
12
2
2020
Statut:
ppublish
Résumé
The effect of putrescine on the dynamics, conformation, and kinetics of acid phosphatase investigated via different experimental and theoretical methods. The Stern-Volmer constants (K
Identifiants
pubmed: 32045610
pii: S0141-8130(19)38890-7
doi: 10.1016/j.ijbiomac.2020.02.057
pii:
doi:
Substances chimiques
Acid Phosphatase
EC 3.1.3.2
Putrescine
V10TVZ52E4
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
90-101Informations de copyright
Copyright © 2020. Published by Elsevier B.V.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare no competing financial interest.