Quantitation of the Nearest-neighbour Effects of Amino Acid Side-Chains that Restrict Conformational Freedom of the Polypeptide Chain using Reversed-Phase Liquid Chromatography of Synthetic Model Peptides with L- and D-amino Acid Substitutions

Lignende værker

• Determination of Intrinsic Hydrophilicity/Hydrophobicity of Amino Acid Side Chains in Peptides in the Absence of Nearest-Neighbor or Conformational Effects
  af: Kovacs, James M., et al.
  Udgivet: (2006)
• Intrinsic Amino Acid Side-Chain Hydrophilicity/Hydrophobicity Coefficients Determined by Reversed-Phase High-Performance Liquid Chromatography of Model Peptides: Comparison with Other Hydrophilicity/Hydrophobicity Scales
  af: Mant, Colin T., et al.
  Udgivet: (2009)
• Structure guided RP-HPLC chromatography of diastereomeric α-helical peptide analogs substituted with single amino acid stereoisomers
  af: Huang, YiBing, et al.
  Udgivet: (2013)
• Two types of lambda polypeptide chains in human immunoglobulins based on an amino acid substitution at position 190.
  af: Appella, E, et al.
  Udgivet: (1967)
• Radical Functionalization of Unsaturated Amino Acids: Synthesis of Side-Chain-Fluorinated, Azido-Substituted, and Hydroxylated Amino Acids
  af: Philip A. P. Reeve, et al.
  Udgivet: (2019-06-01)