Global ITC fitting methods in studies of protein allostery.
about
Integration and global analysis of isothermal titration calorimetry data for studying macromolecular interactions.Entropic Enhancement of Protein-DNA Affinity by Oxygen-to-Sulfur Substitution in DNA Phosphate.Mechanistic Models Fit to Variable Temperature Calorimetric Data Provide Insights into Cooperativity.Applications of isothermal titration calorimetry - the research and technical developments from 2011 to 2015.Biophysical studies suggest a new structural arrangement of crotoxin and provide insights into its toxic mechanism.Applications of NMR and computational methodologies to study protein dynamics.Multi-site binding of epigallocatechin gallate to human serum albumin measured by NMR and isothermal titration calorimetry.Thermodynamic and NMR Assessment of Ligand Cooperativity and Intersubunit Communication in Symmetric Dimers: Application to Thymidylate Synthase.Thermal Activity in Affinity Separation Techniques Such as Liquid-Liquid Extraction Analyzed by Isothermal Titration Calorimetry and Accuracy Analysis of the Technique in the Molar Concentration DomainTheoretical analysis of inducer and operator binding for cyclic-AMP receptor protein mutants
P2860
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P2860
Global ITC fitting methods in studies of protein allostery.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
Global ITC fitting methods in studies of protein allostery.
@en
type
label
Global ITC fitting methods in studies of protein allostery.
@en
prefLabel
Global ITC fitting methods in studies of protein allostery.
@en
P2093
P2860
P1433
P1476
Global ITC fitting methods in studies of protein allostery.
@en
P2093
Anthony Mittermaier
Karine Auclair
Lee Freiburger
P2860
P304
P356
10.1016/J.YMETH.2014.12.018
P577
2015-01-05T00:00:00Z