The F130L mutation in streptavidin reduces its binding affinity to biotin through electronic polarization effect-Reference-Cited by-同舟云学术

The F130L mutation in streptavidin reduces its binding affinity to biotin through electronic polarization effect

Published:2013-09-02 Issue:31 Volume:34 Page:2677-2686
ISSN:0192-8651
Container-title:Journal of Computational Chemistry
language:en
Short-container-title:J. Comput. Chem.

Author:

Zeng Juan¹,Jia Xiangyu¹,Zhang John Z. H.¹²,Mei Ye¹

Affiliation:

1. State Key Laboratory of Precision Spectroscopy, Department of Physics and Institute of Theoretical and Computational Science; East China Normal University; Shanghai 200062 China

2. Department of Chemistry; New York University; New York New York 10003

Publisher

Wiley

Subject

Computational Mathematics,General Chemistry

Reference48 articles.

1. AVIDIN. 1. THE USE OF [14C]BIOTIN FOR KINETIC STUDIES AND FOR ASSAY

2. Thermodynamics of the binding of biotin and some analogues by avidin

3. Avidin

4. [5] Avidin and streptavidin

5. The Origins of Femtomolar Protein−Ligand Binding: Hydrogen-Bond Cooperativity and Desolvation Energetics in the Biotin−(Strept)Avidin Binding Site

Cited by 15 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Better force fields start with better data: A data set of cation dipeptide interactions;Scientific Data;2022-06-17

2. Molecular basis of SMAC-XIAP binding and the effect of electrostatic polarization;Journal of Biomolecular Structure and Dynamics;2020-01-27

3. From Levinthal’s Paradox to the Effects of Cell Environmental Perturbation on Protein Folding;Current Medicinal Chemistry;2020-01-08

4. Entropic effect and residue specific entropic contribution to the cooperativity in streptavidin–biotin binding;Nanoscale;2020

5. In Silico Studies of Crystal Structure of HCV NS5B Polymerase and Inhibitor Complex;Materials Today: Proceedings;2018