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Parameters of helix–coil transition theory for alanine‐based peptides of varying chain lengths in water
TLDR
The success of helix–coil theory in describing the unfolding transitions of short peptides in water indicates that helical propensities, or s values, can be determined from substitution experiments in short alanine‐based peptides. Expand
Calorimetric determination of the enthalpy change for the alpha-helix to coil transition of an alanine peptide in water.
TLDR
The enthalpy change (delta H) accompanying the alpha-helix to random coil transition in water has been determined calorimetrically for a 50-residue peptide of defined sequence that contains primarily alanine, and it is suggested that the side chain has little effect on delta H. Expand
Urea unfolding of peptide helices as a model for interpreting protein unfolding.
TLDR
The result indicates that the interaction between urea and peptide groups accounts for a major part of the denaturing action of urea on proteins, as predicted earlier by some model studies with small molecules. Expand
Kinetics of amide proton exchange in helical peptides of varying chain lengths. Interpretation by the Lifson-Roig equation.
The kinetics of amide proton exchange (1H----2H) have been measured by proton nuclear magnetic resonance spectroscopy for a set of helical peptides with the generic formula Ac-(AAKAA)m Y-NH2 and withExpand
Calorimetric determination of the enthalpy change for the a-helix to coil transition of an alanine peptide in water ( L-alanine helix / peptide hydrogen bond / helix-coil enthalpy )
The enthalpy change (AM) accompanying the a-helix to random coil transition in water has been determined calorimetrically for a 50-residue peptide of defined sequence that contains primarily alanine.Expand
Helix propensities of basic amino acids increase with the length of the side-chain.
TLDR
The helix propensities for these basic amino acids increase with the length of the side-chain in the rank order 2,3-diamino-L-propionic acid < 2,4-d Liamino- L-butyric acid < ornithine < lysine, which parallels the increase in helixpropensities with side- chain length of other polar and charged amino acids. Expand
Nature of the charged-group effect on the stability of the C-peptide helix.
TLDR
The residues responsible for the pH-dependent stability of the helix formed by the isolated C-peptide (residues 1-13 of ribonuclease A) have been identified by chemical synthesis of analogues and measurement of their helix-forming properties and they support the suggestion that the distribution of charged residues in protein helices reflects the helIX-stabilizing propensity of those residues. Expand
Effects of resin swelling and substitution on solid phase synthesis.
TLDR
Effects of resin swelling, uniformity, and substitution on the solid phase synthesis of long, structured and/or branched peptides were evaluated. Expand
Bradykinin antagonists as new drugs for prostate cancer.
TLDR
The established BK antagonists, while less effective against this line of prostate cancer in xenografts in nude mice than against lung cancer, are active and have led the way to development of new peptide and nonpeptide agents for prostate cancer. Expand
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