ArticleJournal of the American Society for Mass Spectrometry1996
Mass spectrometric measurement of changes in protein hydrogen exchange rates that result from point mutations.
Article in Journal of the American Society for Mass Spectrometry, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
6 citing papers in PubMed, 22 citations in OpenAlex.
- Changes in Lysozyme Flexibility upon Mutation Are Frequent, Large and Long-Ranged.PLoS computational biology · 2012Article
- Automatic analysis of hydrogen/deuterium exchange mass spectra of peptides and proteins using calculations of isotopic distributions.Journal of the American Society for Mass Spectrometry · 2001Article
- Inter- and intra-molecular migration of peptide amide hydrogens during electrospray ionization.Journal of the American Society for Mass Spectrometry · 2001Article
- Electrospray ionization mass spectrometry as a tool to analyze hydrogen/deuterium exchange kinetics of transmembrane peptides in lipid bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Fourier transform ion cyclotron resonance mass spectrometric detection of small Ca(2+)-induced conformational changes in the regulatory domain of human cardiac troponin C.Journal of the American Society for Mass Spectrometry · 1999Article
- Zinc-induced conformational changes in the DNA-binding domain of the vitamin D receptor determined by electrospray ionization mass spectrometry.Journal of the American Society for Mass Spectrometry · 1998Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Point mutations, as well as additions or deletions of entire domains, are frequently produced to study protein function; however, to infer function from mutant proteins, it is imperative that their structural integrity be verified. Although detailed structural studies can be performed by using NMR or crystallography, for practical reasons mutant proteins usually are characterized by using less rigorous techniques. Here it is shown that measurement of hydrogen exchange rates via electrospray ionization mass spectrometry is a sensitive and generally applicable method for detection of conformational or dynamic changes that result from point mutations. Hydrogen exchange experiments were performed on a bacterial phosphocarrier protein (HPr) and two variants produced by conversion of either serine-46 to aspartic acid (S46D) or serine-31 to alanine (S31A), where the differences in the ΔG of folding relative to the wild type were 1.5 and 0.5 kcal/mol, respectively. Whereas no significant differences were found for the intact mutant and wild-type proteins, changes in deuterium incorporation could be detected within specific regions produced by peptic proteolysis of the deuterium-labeled proteins. Thus, energetically small changes in conformation (or dynamics) that result from point mutations can be characterized by mass spectrometric measurements of hydrogen exchange rates. Furthermore, these changes can be localized to specific regions within the protein.
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.