Structure and dynamics of peptide-amphiphiles incorporating triple- helical proteinlike molecular architecture

Keyphrases

• Peptide Amphiphiles 100%
• Molecular Architecture 100%
• Protein-like 100%
• Pro-Gly-Pro 58%
• Triple-helical Peptides 25%
• Triple Helix 16%
• Heteronuclear Single Quantum Coherence 16%
• 15N Labeling 16%
• Organized Structure 16%
• Low Temperature 8%
• Structure Function 8%
• Bioactive 8%
• Active Regions 8%
• Biologically Active 8%
• Type IV Collagen 8%
• Thermal Stability 8%
• Helix 8%
• Amino Acid Sequence 8%
• Hexanoic Acid 8%
• Circular Dichroism 8%
• Helical Conformation 8%
• Head Group 8%
• Solution Structure 8%
• Relaxation Measurements 8%
• Targeted Liposomes 8%
• Cross Peak 8%
• Labeled Peptide 8%
• Trimeric 8%
• 15N NMR Spectroscopy 8%
• Coherence Spectrum 8%
• Polymer Assembly 8%
• Three-dimensional Features 8%
• Enhanced Thermal Stability 8%
• N-H Bond 8%
• Amphiphile System 8%
• Acylate 8%

Biochemistry, Genetics and Molecular Biology

• Dynamics 100%
• Peptide Amphiphiles 100%
• Thermostability 16%
• Triple Helix 16%
• Solution and Solubility 8%
• Conformation 8%
• Polymerization 8%
• Type IV Collagen 8%
• N-Terminus 8%
• Peptide Sequence 8%
• Enzyme 8%
• Protein Structure 8%
• C-Terminus 8%
• Structure Activity Relation 8%
• Circular Dichroism 8%
• Hexanoic Acid 8%