L
Lars Andersson
Researcher at University of North Carolina at Chapel Hill
Publications - 6
Citations - 980
Lars Andersson is an academic researcher from University of North Carolina at Chapel Hill. The author has contributed to research in topics: Alcohol dehydrogenase & Aldehyde. The author has an hindex of 6, co-authored 6 publications receiving 953 citations. Previous affiliations of Lars Andersson include Lund University.
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Affinities of Amino Acid Side Chains for Solvent Water
TL;DR: Equilibria of distribution of amino acid side chains, between their dilute aqueous solutions and the vapor phase at 25 degrees C, have been determined by dynamic vapor pressure measurements, and hydration potentials are more closely correlated with the relative tendencies of the various amino acids to appear at the surface of globular proteins than had been evident from earlier distribution studies on the free amino acids.
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alpha-aminoaldehydes: transition state analogue inhibitors of leucine aminopeptidase.
TL;DR: A comparison of binding affinities suggests that L-leucinal forms an inhibitory complex analogous in structure to unstable intermediates and substrate transformation by leucine aminopeptidase, and strengthens the likelihood that this enzyme may act by a double-displacement mechanism.
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Use of secondary isotope effects and varying pH to investigate the mode of binding of inhibitory amino aldehydes by leucine aminopeptidase.
TL;DR: Comparison of pKa values of the model compounds aminoacetone and aminoacetal indicates that the equilibrium constant for hydration of amino aldehydes is reduced by a factor of about 2 when a proton is lost from the alpha-ammonium group near pH 8.
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Coupling of dyes to biopolymers by sensitized photooxidation. Affinity labeling of a binding site in bovine serum albumin.
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A general method of α-aminoaldehyde synthesis using alcohol dehydrogenase
Lars Andersson,Richard Wolfenden +1 more
TL;DR: In this article, α-Amino alcohols with nonpolar side chains were tested as substrates for alcohol dehydrogenase from horse liver in hope of obtaining a new route to antiproteolytic aldehydes.