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Coupling of DNA binding and helicase activity is mediated by a conserved loop in the MCM protein
TLDR
Mutational analysis and biochemical characterization of the conserved residues suggest that the loop participates in communication between the N-terminal portion of the helicase and the C-Terminal catalytic domain of the eukaryotic enzyme. Expand
Bound water molecules and conformational stabilization help mediate an antigen-antibody association.
TLDR
Structural analysis of the Fv fragment of the anti-hen egg white lysozyme antibody D1.3 reveals a role for solvent molecules in stabilizing the complex and provides a molecular basis for understanding the thermodynamic forces which drive the association reaction. Expand
In Vivo Brain Water Determination by T1 Measurements: Effect of Total Water Content, Hydration Fraction, and Field Strength
TLDR
It is concluded that routine, accurate, and noninvasive brain water measurements are possible by magnetic resonance imaging in a clinical environment. Expand
The Hydrophobic Nature of GroEL-Substrate Binding (*)
TLDR
The negative heat capacity change provides strong evidence for the role of hydrophobic interactions as the driving force for the association of these substrates with the GroEL chaperonin. Expand
The ABRF-MIRG'02 study: assembly state, thermodynamic, and kinetic analysis of an enzyme/inhibitor interaction.
TLDR
A standard model system for evaluating the capabilities of core facilities to implement analytical ultracentrifugation, isothermal titration calorimetry, and surface plasmon resonance technologies is developed and distributed to operators of AUC, ITC, and SPR. Expand
Thermodynamics of monosaccharide binding to concanavalin A, pea (Pisum sativum) lectin, and lentil (Lens culinaris) lectin.
TLDR
Differential scanning calorimetry measurements on the thermal denaturation of the lectins and their carbohydrate complexes show that the Con A tetramer dissociates into monomers, while the pea and lentil lectin dimers dissociate into two submonomer fragments. Expand
Thermodynamics of Monosaccharide and Disaccharide Binding to Erythrina corallodendron Lectin*
TLDR
Differential scanning calorimetry measurements show that denaturation of the ECorL dimer results in dissociation into its monomer subunits, well below the 344-360 K denaturation temperature of other legume lectins of similar size and tertiary structure, undoubtedly due to the difference in its quaternary structure relative to other legumes lectins. Expand
Thermodynamics of antigen-antibody binding using specific anti-lysozyme antibodies.
TLDR
The apolar surface areas buried at the binding sites estimated from the heat capacity changes indicate that the binding reactions are primarily hydrophobic, contrary to the mainly observed enthalpy-driven nature of the reactions. Expand
Thermodynamics of bovine spleen galectin-1 binding to disaccharides: correlation with structure and its effect on oligomerization at the denaturation temperature.
TLDR
The binding enthalpies calculated from changes in the solvent-accessible surface areas of the galectin binding site upon binding of the disaccharide were in close agreement with the experimental values for lactose, lactulOSE, lacto-N-biose, and N-acetyllactosamine, all of which exhibit binding ent Halpies >-36 kJ mol-1. Expand
Thermodynamics of Cyclic Nucleotide Binding to the cAMP Receptor Protein and Its T127L Mutant (*)
TLDR
The point mutation, T127L, switches off the cooperativity between the cAMP ligated binding sites without affecting the binding constant of cAMP and changes the specificity of the protein so that transcription is now activated only upon cGMP binding. Expand
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