Slow Histidine H/D Exchange Protocol for Thermodynamic Analysis of Protein Folding and Stability Using Mass Spectrometry-Reference-Cited by-同舟云学术

Slow Histidine H/D Exchange Protocol for Thermodynamic Analysis of Protein Folding and Stability Using Mass Spectrometry

Published:2012-01-18 Issue:3 Volume:84 Page:1653-1660
ISSN:0003-2700
Container-title:Analytical Chemistry
language:en
Short-container-title:Anal. Chem.

Author:

Tran Duc T.¹,Banerjee Sambuddha²,Alayash Abdu I.³,Crumbliss Alvin L.²,Fitzgerald Michael C.¹²

Affiliation:

1. Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27708, United States

2. Department of Chemistry, Duke University, Durham, North Carolina 27708, United States

3. Laboratory of Biochemistry and Vascular Biology, Center of Biologics Evaluation and Research, Food and Drug Administration, Bethesda, Maryland 20892, United States

Publisher

American Chemical Society (ACS)

Subject

Analytical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ac202927p

Reference31 articles.

1. Binding constant determination of high-affinity protein–ligand complexes by electrospray ionization mass spectrometry and ligand competition

2. Mass spectrometric determination of association constants of adenylate kinase with two noncovalent inhibitors

3. Measurement of Macromolecular Binding Using Electrospray Mass Spectrometry. Determination of Dissociation Constants for Oligonucleotide: Serum Albumin Complexes

4. A study of Src SH2 domain protein-phosphopeptide binding interactions by electrospray ionization mass spectrometry

5. A quantitative, high-throughput screen for protein stability

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