Determination of Intrinsic Hydrophilicity/Hydrophobicity of Amino Acid Side Chains in Peptides in the Absence of Nearest-Neighbor or Conformational Effects

Lignende værker

• 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)
• 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
  af: Kovacs, James M., et al.
  Udgivet: (2006)
• Requirements for prediction of peptide retention time in reversed-phase high-performance liquid chromatography: hydrophilicity/hydrophobicity of side-chains at the N- and C-termini of peptides are dramatically affected by the end-groups and location
  af: Tripet, Brian, et al.
  Udgivet: (2006)
• Context-dependent effects on the hydrophilicity/hydrophobicity of side-chains during reversed-phase high-performance liquid chromatography: Implications for prediction of peptide retention behaviour
  af: Mant, C.T., et al.
  Udgivet: (2006)
• Mixed-mode hydrophilic interaction/cation-exchange chromatography: Separation of complex mixtures of peptides of varying charge and hydrophobicity
  af: Mant, Colin T., et al.
  Udgivet: (2008)