(Q44084246)

29 November 2017

title

Characterization of parvalbumin and polcalcin divalent ion binding by isothermal titration calorimetry (English)

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29 November 2017

Michael T Henzl

1

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29 November 2017

language of work or name

English

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publication date

1 January 2009

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29 November 2017

published in

Methods in Enzymology

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29 November 2017

volume

455

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29 November 2017

page(s)

259-297

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Global analysis of biochemical and biophysical data

29 November 2017

cites work

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7 January 2021

Isothermal titration calorimetry: experimental design, data analysis, and probing macromolecule/ligand binding and kinetic interactions

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7 January 2021

Thermodynamic Quantities for the Ionization Reactions of Buffers

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7 January 2021

Magnesium and calcium binding to parvalbumins: evidence for differences between parvalbumins and an explanation of their relaxing function

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7 January 2021

Structure and function of parvalbumin

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Rat alpha- and beta-parvalbumins: comparison of their pentacarboxylate and site-interconversion variants

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7 January 2021

Divalent ion binding properties of the timothy grass allergen, Phl p 7.

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Introduction of a fifth carboxylate ligand heightens the affinity of the oncomodulin CD and EF sites for Ca2+

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7 January 2021

Thermodynamic studies of the interaction of trp aporepressor with tryptophan analogs.

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Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques

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7 January 2021

Parameter estimation by least-squares methods

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Sensing the heat: the application of isothermal titration calorimetry to thermodynamic studies of biomolecular interactions

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7 January 2021

Direct measurement of protein binding energetics by isothermal titration calorimetry

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7 January 2021

Crystal structure of a high-affinity variant of rat alpha-parvalbumin

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Proton NMR studies of synthetic peptide analogs of calcium-binding site III of rabbit skeletal troponin C: Effect on the lanthanum affinity of the interchange of aspartic acid and asparagine residues at the metal ion coordinating positions

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The Ca2+(-)binding proteins parvalbumin and oncomodulin and their genes: new structural and functional findings

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An improved function for fitting sedimentation velocity data for low-molecular-weight solutes

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Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling

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Exact analysis of competition ligand binding by displacement isothermal titration calorimetry.

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Thermodynamics of inhibitor binding to the catalytic site of glucoamylase from Aspergillus niger determined by displacement titration calorimetry.

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Crystal structures of the helix-loop-helix calcium-binding proteins

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Crystal structure of the D94S/G98E variant of rat alpha-parvalbumin. An explanation for the reduced divalent ion affinity

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7 January 2021

Statistical error in isothermal titration calorimetry

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7 January 2021

Molecular, structural, and immunologic relationships between different families of recombinant calcium-binding pollen allergens

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Calcium-binding allergens: from plants to man

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Three-dimensional structure of the panallergen Phl p 7

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7 January 2021

10.1016/S0076-6879(08)04210-9

Identifiers

DOI

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29 November 2017

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