Role of backbone solvation and electrostatics in generating preferred peptide backbone conformations: Distributions of phi
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference31 articles.
1. Comparison between the φ Distribution of the Amino Acids in the Protein Database and NMR Data Indicates that Amino Acids have Various φ Propensities in the Random Coil Conformation
2. Analysis of Main Chain Torsion Angles in Proteins: Prediction of NMR Coupling Constants for Native and Random Coil Conformations
3. Contact Electron‐Spin Coupling of Nuclear Magnetic Moments
4. Intrinsic φ,ψ propensities of amino acids, derived from the coil regions of known structures
5. The Configuration of Random Polypeptide Chains. I. Experimental Results
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