Protein Flexibility and Conformational Entropy in Ligand Design Targeting the Carbohydrate Recognition Domain of Galectin-3-Reference-Cited by-同舟云学术

Protein Flexibility and Conformational Entropy in Ligand Design Targeting the Carbohydrate Recognition Domain of Galectin-3

Published:2010-09-28 Issue:41 Volume:132 Page:14577-14589
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Diehl Carl¹,Engström Olof¹,Delaine Tamara¹,Håkansson Maria¹,Genheden Samuel¹,Modig Kristofer¹,Leffler Hakon¹,Ryde Ulf¹,Nilsson Ulf J.¹,Akke Mikael¹

Affiliation:

1. Center for Molecular Protein Science, Biophysical Chemistry, Lund University, P.O. Box 124, SE-22100 Lund, Sweden, Organic Chemistry, Lund University, P.O. Box 124, SE-22100 Lund, Sweden, SARomics Biostructures AB, P.O. Box 724, SE-22007 Lund, Sweden, Theoretical Chemistry, Lund University, P.O. Box 124, SE-22100 Lund, Sweden, and Section MIG, Department of Laboratory Medicine, Lund University, Sölvegatan 23, SE-22362 Lund, Sweden

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja105852y

Reference112 articles.

1. Do enthalpy and entropy distinguish first in class from best in class?

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4. Direct measurement of protein binding energetics by isothermal titration calorimetry

5. The Thermodynamics of Protein–Ligand Interaction and Solvation: Insights for Ligand Design

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