¹H-¹⁵N NMR dynamic study of an isolated α-helical peptide (1-36)-bacteriorhodopsin reveals the equilibrium helix-coil transitions

Keyphrases

• Dynamic Study 100%
• Picosecond 100%
• Bacteriorhodopsin 100%
• 15N NMR 100%
• Helical Peptides 100%
• Helix-coil Transition 100%
• Dynamic NMR 100%
• Heteronuclear 66%
• Order Parameter 66%
• Statistical Analysis 33%
• Exchange Processes 33%
• Chloroform 33%
• Magnetic Field 33%
• Helix 33%
• Lower Order 33%
• Freeform 33%
• Pico 33%
• Extended Model 33%
• Spectral Density 33%
• C-terminus 33%
• Membrane Protein 33%
• Longitudinal Relaxation 33%
• Micro-nano 33%
• Backbone Dynamics 33%
• 15N NMR Spectroscopy 33%
• Transverse Relaxation 33%
• Peptide Helices 33%
• Conformational Exchange 33%
• Methanol Blends 33%
• Steady-state NOE 33%
• Nanosecond Time Scale 33%
• Backbone Amide 33%
• Microsecond Timescale 33%

Chemistry

• Order Parameter 100%
• 15N NMR Spectroscopy 100%
• Methanol 50%
• Relaxation 50%
• Nuclear Overhauser Effect 50%
• Carboxamide 50%
• Magnetic Field 50%
• Chloroform 50%

Biochemistry, Genetics and Molecular Biology

• Motion 100%
• Bacteriorhodopsin 100%
• Dynamics 75%
• Nuclear Magnetic Resonance Spectroscopy 25%
• Magnetic Field 25%
• Chloroform 25%
• C-Terminus 25%
• Steady State 25%