Unknown

Dataset Information

0

HDXFinder: automated analysis and data reporting of deuterium/hydrogen exchange mass spectrometry.


ABSTRACT: Hydrogen/deuterium exchange in combination with mass spectrometry (H/D MS) is a sensitive technique for detection of changes in protein conformation and dynamics. However, wide application of H/D MS has been hindered, in part, by the lack of computational tools necessary for efficient analysis of the large data sets associated with this technique. We report a novel web-based application for automatic analysis of H/D MS experimental data. This application relies on the high resolution of mass spectrometers to extract all isotopic envelopes before correlating these envelopes with individual peptides. Although a fully automatic analysis is possible, a variety of graphical tools are included to aid in the verification of correlations and rankings of the isotopic peptide envelopes. As a demonstration, the rate constants for H/D exchange of peptides from rabbit muscle pyruvate kinase are mapped onto the structure of this protein.

SUBMITTER: Miller DE 

PROVIDER: S-EPMC3839233 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

HDXFinder: automated analysis and data reporting of deuterium/hydrogen exchange mass spectrometry.

Miller Danny E DE   Prasannan Charulata B CB   Villar Maria T MT   Fenton Aron W AW   Artigues Antonio A  

Journal of the American Society for Mass Spectrometry 20111115 2


Hydrogen/deuterium exchange in combination with mass spectrometry (H/D MS) is a sensitive technique for detection of changes in protein conformation and dynamics. However, wide application of H/D MS has been hindered, in part, by the lack of computational tools necessary for efficient analysis of the large data sets associated with this technique. We report a novel web-based application for automatic analysis of H/D MS experimental data. This application relies on the high resolution of mass spe  ...[more]

Similar Datasets

| S-EPMC10928179 | biostudies-literature
| S-EPMC4018513 | biostudies-literature
| S-EPMC6614034 | biostudies-literature
| S-EPMC9996604 | biostudies-literature
| S-EPMC10034745 | biostudies-literature
| S-EPMC3113475 | biostudies-literature
| S-EPMC5054352 | biostudies-literature
| S-EPMC2901854 | biostudies-literature
| S-EPMC6736138 | biostudies-literature
| S-EPMC3796066 | biostudies-literature