Folding of βpep-4 β-sheet sandwich dimers and tetramers is influenced by aliphatic hydrophobic residues at the intersubunit interface

Keyphrases

• Leucine 100%
• Hydrophobic Residues 100%
• Self-association 66%
• Pulsed Electric Field 33%
• Peptide Concentration 33%
• Diffusion Coefficient 33%
• Valine 33%
• NOESY 33%
• Sheet Structure 33%
• Monomer-dimer 33%
• Thermodynamic Stability 33%
• Dimer Formation 33%
• Field Gradient 33%
• Random Coil 33%
• Gradient NMR 33%
• Equilibrium Association Constant 33%
• Tetramer Formation 33%
• Tetramer Stability 33%
• Double Sites 33%
• Designed Peptide 33%

Biochemistry, Genetics and Molecular Biology

• Peptide 100%
• Leucine 50%
• Biochemistry 25%
• Dimerization 25%
• Nuclear Overhauser Effect Spectroscopy 25%
• Diffusion Coefficient 25%
• Pulse Rate 25%
• Valine 25%
• Alanine 25%
• Isoleucine 25%
• Thermodynamics 25%