Modeling data from titration, amide H/D exchange, and mass spectrometry to obtain protein-ligand binding constants (Q30909781)

27 June 2017

title

Modeling data from titration, amide H/D exchange, and mass spectrometry to obtain protein-ligand binding constants (English)

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27 June 2017

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Mei M Zhu

1

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27 June 2017

Don L Rempel

series ordinal

2

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27 June 2017

Michael L Gross

series ordinal

3

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27 June 2017

publication date

1 March 2004

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Journal of the American Society for Mass Spectrometry

27 June 2017

published in

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27 June 2017

volume

15

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27 June 2017

issue

3

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27 June 2017

page(s)

388-397

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Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation

27 June 2017

cites work

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Interfacial positioning and stability of transmembrane peptides in lipid bilayers studied by combining hydrogen/deuterium exchange and mass spectrometry

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Human recombinant [C22A] FK506-binding protein amide hydrogen exchange rates from mass spectrometry match and extend those from NMR

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Why, when, and how biochemists should use least squares

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Outliers and robust parameter estimation

21 January 2018

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21 January 2018

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Probing Ca2+-induced conformational changes in porcine calmodulin by H/D exchange and ESI-MS: effect of cations and ionic strength

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Affinity of fatty acid for (r)rat intestinal fatty acid binding protein:further examination

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12 December 2020

A computational approach to the spectrophotometric determination of stability constants-II Application to metalloporphyrin-axial ligand interactions in non-aqueous solvents

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12 December 2020

Calcium binding to calmodulin and its globular domains

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12 December 2020

Amide hydrogen exchange determined by mass spectrometry: application to rabbit muscle aldolase

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Electrospray ionization mass spectrometry as a tool to analyze hydrogen/deuterium exchange kinetics of transmembrane peptides in lipid bilayers.

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Identifiers

DOI

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Dimensions Publication ID

27 June 2017

1023186039

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