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Complex kinetics and residual structure in the thermal unfolding of yeast triosephosphate isomerase.Structural energetics of protein-carbohydrate interactions: Insights derived from the study of lysozyme binding to its natural saccharide inhibitors.Surface Tension of Organic Liquids Using the OPLS/AA Force Field.Binding energetics of the inhibitor cystatin to the cysteine proteinase actinidin.Conserved cysteine 126 in triosephosphate isomerase is required not for enzymatic activity but for proper folding and stability.Effect of a specific inhibitor on the unfolding and refolding kinetics of dimeric triosephosphate isomerase: establishing the dimeric and similarly structured nature of the main transition states on the forward and backward reactions.Using evolutionary changes to achieve species-specific inhibition of enzyme action — studies with triosephosphate isomeraseDifferential inactivation of rabbit and yeast triosephosphate isomerase: effect of oxidations produced by chloramine-TThermal denaturation of β-glucosidase B from Paenibacillus polymyxa proceeds through a Lumry-Eyring mechanismAdditive effect of single amino acid replacements on the kinetic stability of β-glucosidase BBinding thermodynamics of phosphorylated inhibitors to triosephosphate isomerase and the contribution of electrostatic interactionsStabilized Human Cystatin C Variant L47C/G69C Is a Better Reporter Than the Wild-Type Inhibitor for Characterizing the Thermodynamics of Binding to Cysteine ProteasesCorrection to: Stabilized Human Cystatin C, Variant L47C/G69C, is a Better Reporter than the Wild-type Inhibitor for Characterizing the Thermodynamics of Binding to Cysteine Proteases
P50
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P50
description
researcher
@en
wetenschapper
@nl
name
R A Zubillaga
@en
R A Zubillaga
@nl
type
label
R A Zubillaga
@en
R A Zubillaga
@nl
prefLabel
R A Zubillaga
@en
R A Zubillaga
@nl
P106
P31
P496
0000-0003-1919-5015