SRLS Analysis of ¹⁵N-¹H NMR Relaxation from the Protein S100A1: Dynamic Structure, Calcium Binding, and Related Changes in Conformational Entropy

Keyphrases

• Dynamic Structure 100%
• Local Structure Analysis 100%
• Conformational Entropy 100%
• Calcium Binding 100%
• 1H NMR Relaxation 100%
• S100A1 100%
• EF-hand 66%
• Local Structure 50%
• N-H Bond 33%
• Helix 33%
• Tumbling 33%
• Extended Model 33%
• Local Diffusion 16%
• Conformational Exchange 16%
• Local Potential 16%
• Linker 16%
• Binding Mechanism 16%
• Local Motion 16%
• Imperfection 16%
• Diffusion Tensor 16%
• Free Energy 16%
• Structural Information 16%
• Kinetic Data 16%
• Model-free Methods 16%
• NMR Relaxation 16%
• Slowing down 16%
• Bound Form 16%
• Fit Parameters 16%
• Data Fitting 16%
• Geometric Information 16%
• Model Experimental 16%
• Parameter Combination 16%
• Entropic Contribution 16%
• Amide Nitrogen 16%
• H-NMR 16%
• Structural Kinetics 16%
• Binding Information 16%
• Helix-loop-helix Motifs 16%
• Calcium-free 16%

Biochemistry, Genetics and Molecular Biology

• Structure Analysis 100%
• Conformational Entropy 100%
• Calcium Binding 100%
• EF Hand 66%
• Motion 50%
• Facilitated Diffusion 33%
• N-Terminus 33%
• C-Terminus 16%