H/D exchange- and mass spectrometry-based strategy for the thermodynamic analysis of protein-ligand binding.

H/D exchange- and mass spectrometry-based strategy for the thermodynamic analysis of protein-ligand binding. Research Abstract Details 

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H/D exchange- and mass spectrometry-based strategy for the thermodynamic analysis of protein-ligand binding. Abstract Text:

Liangjie Tang,Erin D Hopper,Yan Tong,Jack D Sadowsky,Kimberly J Peterson,Samuel H Gellman,Michael C Fitzgerald,

The equilibrium unfolding properties of four model protein systems were characterized using SUPREX (stability of unpurified proteins from rates of H/D exchange). SUPREX is an H/D exchange- and mass spectrometry-based technique for measuring the free energy (DeltaGf) and m-value (deltaDeltaGf/delta[denaturant]) associated with the folding/unfolding reaction of a protein. The model proteins in this study (calmodulin, carbonic anhydrase II, RmlB, Bcl-xL) were chosen to test the applicability of SUPREX to the thermodynamic analysis of larger (> approximately 15 kDa) or multidomain proteins. In the absence of ligand, DeltaGf and m-values for these proteins could not be evaluated using the conventional data acquisition and analysis methods previously established for SUPREX. However, ligand-bound forms of the proteins were amenable to conventional SUPREX analyses, and it was possible to evaluate reasonably accurate and precise binding free energies of selected ligands. In some cases, protein-ligand dissociation constants (Kd values) could also be ascertained. The SUPREX-derived binding free energies and Kd values evaluated here were in good agreement with those reported on the same complexes using other techniques.

H/D exchange- and mass spectrometry-based strategy for the thermodynamic analysis of protein-ligand binding. Publishing Authors By Initials

L Tang,ED Hopper,Y Tong,JD Sadowsky,KJ Peterson,SH Gellman,MC Fitzgerald,

For similar peptides: intracellular signaling peptides and proteins: apoptosis regulatory proteins: proto-oncogene proteins c-bcl-2: bcl-x protein research abstracts see: peptides: intracellular signaling peptides and proteins: apoptosis regulatory proteins: proto-oncogene proteins c-bcl-2: bcl-x protein research

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H/D exchange- and mass spectrometry-based strategy for the thermodynamic analysis of protein-ligand binding. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Analytical chemistry

VOLUME: 79

Page Numbers: 5869-77

Journal Abbreviation: Anal. Chem.

ISSN: 0003-2700

DAY: 21

MONTH: 06

YEAR: 2007

H/D exchange- and mass spectrometry-based strategy for the thermodynamic analysis of protein-ligand binding. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 370536

H/D exchange- and mass spectrometry-based strategy for the thermodynamic analysis of protein-ligand binding. Keywords Mesh Terms:

KEYWORDS: bcl-X Protein

MESH TERMS: chemistry

Chemical & Substance for Abstract: H/D exchange- and mass spectrometry-based strategy for the thermodynamic analysis of protein-ligand binding. Information

Substance Name: dTDPglucose 4,6-dehydratase

Registry Number: EC 4.2.1.46

Grant and Affiliation Information for H/D exchange- and mass spectrometry-based strategy for the thermodynamic analysis of protein-ligand binding.

AFFILIATION: Department of Chemistry, Duke University, Durham, North Carolina 27708, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM56414

ACRONYM: GM

MEDLINETA: Anal Chem

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