Next Article in Journal / Special Issue
Electrophoretic Extraction and Proteomic Characterization of Proteins Buried in Marine Sediments
Previous Article in Journal
A Size Exclusion HPLC Method for Evaluating the Individual Impacts of Sugars and Organic Acids on Beverage Global Taste by Means of Calculated Dose-Over-Threshold Values
Previous Article in Special Issue
Exhaled Breath Condensate for Proteomic Biomarker Discovery
Article Menu

Export Article

From the first issue of 2016, Chromatography has changed its name to Separations.

Open AccessTechnical Note
Chromatography 2014, 1(4), 159-175; doi:10.3390/chromatography1040159

High-Throughput Mass Spectrometry Applied to Structural Genomics

Structural Genomics Consortium, University of Oxford, Old Road Campus Research Building, Roosevelt Drive, Oxford OX3 7DQ, UK
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Received: 1 July 2014 / Revised: 3 September 2014 / Accepted: 11 September 2014 / Published: 9 October 2014
View Full-Text   |   Download PDF [1100 KB, uploaded 9 October 2014]   |  

Abstract

Mass spectrometry (MS) remains under-utilized for the analysis of expressed proteins because it is inaccessible to the non-specialist, and sample-turnaround from service labs is slow. Here, we describe 3.5 min Liquid-Chromatography (LC)-MS and 16 min LC-MSMS methods which are tailored to validation and characterization of recombinant proteins in a high throughput structural biology pipeline. We illustrate the type and scope of MS data typically obtained from a 96-well expression and purification test for both soluble and integral membrane proteins (IMPs), and describe their utility in the selection of constructs for scale-up structural work, leading to cost and efficiency savings. We propose that value of MS data lies in how quickly it becomes available and that this can fundamentally change the way in which it is used. View Full-Text
Keywords: high-throughput; mass spectrometry; protein expression; structural genomics; integral membrane protein (IMP); post-translational modification (PTM); intact mass high-throughput; mass spectrometry; protein expression; structural genomics; integral membrane protein (IMP); post-translational modification (PTM); intact mass
Figures

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Chalk, R.; Berridge, G.; Shrestha, L.; Strain-Damerell, C.; Mahajan, P.; Yue, W.W.; Gileadi, O.; Burgess-Brown, N.A. High-Throughput Mass Spectrometry Applied to Structural Genomics. Chromatography 2014, 1, 159-175.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Chromatography EISSN 2227-9075 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top