Conformational distributions of denatured and unstructured proteins are similar to those of 20 × 20 blocked dipeptides

Keyphrases

• Amino Acids 100%
• Denatured Protein 100%
• Conformational Distribution 100%
• Blocked Dipeptide 100%
• Intrinsically Unstructured Protein 100%
• Lysozyme 66%
• Conformational Preferences 66%
• Oligopeptides 66%
• Chemical Shift 66%
• Escherichia Coli 33%
• Unfolded Proteins 33%
• Amino Acid Side Chains 33%
• Solvation Environment 33%
• Amide Proton 33%
• Intrinsically Disordered 33%
• NMR Properties 33%
• Unstructured Domain 33%
• 1H nuclear Magnetic Resonance (1H NMR) 33%
• Coupling Constant 33%
• Dipeptide 33%
• Scalar Coupling Constant 33%
• Neighborhood Interaction 33%
• Conformational Propensities 33%
• Hepatitis C Virus 33%
• Natively Unfolded Protein 33%
• Interaction Effect 33%
• Proton-proton 33%
• NMR Experiments 33%
• Intracellular Domain 33%
• Outer Membrane Protein OmpX 33%

Biochemistry, Genetics and Molecular Biology

• Oligopeptide 50%