Structural and energetic requirements for a second binding site at the dimeric β-lactoglobulin interface-Reference-Cited by-同舟云学术

Structural and energetic requirements for a second binding site at the dimeric β-lactoglobulin interface

Published:2016-01-06 Issue:9 Volume:34 Page:1884-1902
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Bello Martiniano¹

Affiliation:

1. Laboratorio de Modelado Molecular, Bioinformática y Diseño de Fármacos de la Escuela Superior de Medicina, Instituto Politécnico Nacional, Plan de San Luis Y Diaz Mirón S/N, Col. Casco de Santo Tomas, CP 11340 México, D. F., Mexico

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/07391102.2015.1094413

Reference63 articles.

1. Interaction of bovine -lactalbumin with fatty acids as determined by partition equilibrium and fluorescence spectroscopy

2. Bovine β-lactoglobulin acts as an acid-resistant drug carrier by exploiting its diverse binding regions

3. Binding free energy calculations between bovine β-lactoglobulin and four fatty acids using the MMGBSA method

4. Simulation of the cavity-binding site of three bacterial multicopper oxidases upon complex stabilization: interactional profile and electron transference pathways

5. Ligand entry into the calyx of β-lactoglobulin

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