Pages that link to "Q30559566"

The following pages link to Principal component analysis of chemical shift perturbation data of a multiple-ligand-binding system for elucidation of respective binding mechanism. (Q30559566):

Displaying 13 items.

• Binding Isotherms and Time Courses Readily from Magnetic Resonance (Q27301803) (← links)
• Epicatechin-induced conformational changes in β-lactoglobulin B monitored by FT-IR spectroscopy. (Q30357041) (← links)
• Tracking Equilibrium and Nonequilibrium Shifts in Data with TREND. (Q31156765) (← links)
• NMR mapping of protein conformational landscapes using coordinated behavior of chemical shifts upon ligand binding (Q33983082) (← links)
• Network of long-range concerted chemical shift displacements upon ligand binding to human angiogenin (Q35236825) (← links)
• Protein-Inhibitor Interaction Studies Using NMR (Q36036813) (← links)
• Applications of NMR and computational methodologies to study protein dynamics (Q39291879) (← links)
• Computational and Experimental Studies of ADP-Ribosylation (Q40127884) (← links)
• Increased hydrophobic surface exposure in the cataract-related G18V variant of human γS-crystallin. (Q40440699) (← links)
• Multiple Ligand-Bound States of a Phosphohexomutase Revealed by Principal Component Analysis of NMR Peak Shifts (Q41010274) (← links)
• 2D (1)H(N), (15)N Correlated NMR Methods at Natural Abundance for Obtaining Structural Maps and Statistical Comparability of Monoclonal Antibodies (Q46656897) (← links)
• Deciphering the Multisite Interactions of a Protein and Its Ligand at Atomic Resolution by Using Sensitive Paramagnetic Effects. (Q51110240) (← links)
• Sertraline, chlorprothixene, and chlorpromazine characteristically interact with the REST-binding site of the corepressor mSin3, showing medulloblastoma cell growth inhibitory activities (Q58743854) (← links)