Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Click Me!

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 5 November 1993:
Vol. 262. no. 5135, pp. 896 - 900
DOI: 10.1126/science.8235611
Prev | Table of Contents | Next

Articles

Science, Vol 262, Issue 5135, 896-900
Copyright © 1993 by American Association for the Advancement of Science

articles

Detection of transient protein folding populations by mass spectrometry

A Miranker, CV Robinson, SE Radford, RT Aplin, and CM Dobson

Oxford Centre for Molecular Sciences, Oxford University, United Kingdom.

Hydrogen-deuterium exchange measurements are becoming increasingly important in studies of the dynamics of protein molecules and, particularly, of their folding behavior. Electrospray ionization mass spectrometry (ESI-MS) has been used to obtain the distribution of masses within a population of protein molecules that had undergone hydrogen exchange in solution. This information is complementary to that from nuclear magnetic resonance spectroscopy (NMR) experiments, which measure the average occupancy of individual sites over the distribution of protein molecules. In experiments with hen lysozyme, a combination of ESI-MS and NMR was used to distinguish between alternative mechanisms of hydrogen exchange, providing insight into the nature and populations of transient folding intermediates. These results have helped to detail the pathways available to a protein during refolding.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Scope and utility of hydrogen exchange as a tool for mapping landscapes.
S. S. Jaswal and A. D. Miranker (2007)
Protein Sci. 16, 2378-2390
   Abstract »    Full Text »    PDF »
Structural Characterization of the Human Eukaryotic Initiation Factor 3 Protein Complex by Mass Spectrometry.
E. Damoc, C. S. Fraser, M. Zhou, H. Videler, G. L. Mayeur, J. W. B. Hershey, J. A. Doudna, C. V. Robinson, and J. A. Leary (2007)
Mol. Cell. Proteomics 6, 1135-1146
   Abstract »    Full Text »    PDF »
A unified mechanism for protein folding: Predetermined pathways with optional errors.
M. M.G. Krishna and S. W. Englander (2007)
Protein Sci. 16, 449-464
   Abstract »    Full Text »    PDF »
Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip..
D. D. Weis, P. Kjellen, B. M. Sefton, and J. R. Engen (2006)
Protein Sci. 15, 2402-2410
   Abstract »    Full Text »    PDF »
Enhanced picture of protein-folding intermediates using organic solvents in H/D exchange and quench-flow experiments.
C. Nishimura, H. J. Dyson, and P. E. Wright (2005)
PNAS 102, 4765-4770
   Abstract »    Full Text »    PDF »
Conformational analysis of HAMLET, the folding variant of human {alpha}-lactalbumin associated with apoptosis.
A. Casbarra, L. Birolo, G. Infusini, F. Dal Piaz, M. Svensson, P. Pucci, C. Svanborg, and G. Marino (2004)
Protein Sci. 13, 1322-1330
   Abstract »    Full Text »    PDF »
Hydrogen/deuterium exchange studies of native rabbit MM-CK dynamics.
H. Mazon, O. Marcillat, E. Forest, and C. Vial (2004)
Protein Sci. 13, 476-486
   Abstract »    Full Text »    PDF »
Mass Spectrometric Approaches Using Electrospray Ionization Charge States and Hydrogen-Deuterium Exchange for Determining Protein Structures and Their Conformational Changes.
X. Yan, J. Watson, P. S. Ho, and M. L. Deinzer (2004)
Mol. Cell. Proteomics 3, 10-23
   Abstract »    Full Text »    PDF »
Simulations of Human Lysozyme: Probing the Conformations Triggering Amyloidosis.
G. Moraitakis and J. M. Goodfellow (2003)
Biophys. J. 84, 2149-2158
   Abstract »    Full Text »    PDF »
Probing metal ion binding and conformational properties of the colicin E9 endonuclease by electrospray ionization time-of-flight mass spectrometry.
E. T.J. van den Bremer, W. Jiskoot, R. James, G. R. Moore, C. Kleanthous, A. J.R. Heck, and C. S. Maier (2002)
Protein Sci. 11, 1738-1752
   Abstract »    Full Text »    PDF »
Conformational changes in chemically modified Escherichia coli thioredoxin monitored by H/D exchange and electrospray ionization mass spectrometry.
M.-Y. Kim, C. S. Maier, D. J. Reed, and M. L. Deinzer (2002)
Protein Sci. 11, 1320-1329
   Abstract »    Full Text »    PDF »
Structural features of interferon-{gamma} aggregation revealed by hydrogen exchange.
S. A. Tobler and E. J. Fernandez (2002)
Protein Sci. 11, 1340-1352
   Abstract »    Full Text »    PDF »
Structural Characterization of the M* Partly Folded Intermediate of Wild Type and P138A Aspartate Aminotransferase from Escherichia coli.
L. Birolo, F. Dal Piaz, P. Pucci, and G. Marino (2002)
J. Biol. Chem. 277, 17428-17437
   Abstract »    Full Text »    PDF »
Thermodynamic stability measurements on multimeric proteins using a new H/D exchange- and matrix-assisted laser desorption/ionization (MALDI) mass spectrometry-based method.
K. D. Powell, T. E. Wales, and M. C. Fitzgerald (2002)
Protein Sci. 11, 841-851
   Abstract »    Full Text »    PDF »
Long-Range Interactions Within a Nonnative Protein.
J. Klein-Seetharaman, M. Oikawa, S. B. Grimshaw, J. Wirmer, E. Duchardt, T. Ueda, T. Imoto, L. J. Smith, C. M. Dobson, and H. Schwalbe (2002)
Science 295, 1719-1722
   Abstract »    Full Text »    PDF »
Detecting structural changes in viral capsids by hydrogen exchange and mass spectrometry.
L. Wang, L. C. Lane, and D. L. Smith (2001)
Protein Sci. 10, 1234-1243
   Abstract »    Full Text »    PDF »
Detection and selective dissociation of intact ribosomes in a mass spectrometer.
A. A. Rostom, P. Fucini, D. R. Benjamin, R. Juenemann, K. H. Nierhaus, F. U. Hartl, C. M. Dobson, and C. V. Robinson (2000)
PNAS 97, 5185-5190
   Abstract »    Full Text »    PDF »
Direct Kinetic Evidence for Folding via a Highly Compact, Misfolded State.
M. J. Pandya, P. B. Williams, C. E. Dempsey, P. R. Shewry, and A. R. Clarke (1999)
J. Biol. Chem. 274, 26828-26837
   Abstract »    Full Text »    PDF »
An entropy criterion to detect minimally frustrated intermediates in native proteins.
M. Compiani, P. Fariselli, P. L. Martelli, and R. Casadio (1998)
PNAS 95, 9290-9294
   Abstract »    Full Text »    PDF »
Mass spectrometry of ribosomes and ribosomal subunits.
D. R. Benjamin, C. V. Robinson, J. P. Hendrick, F. U. Hartl, and C. M. Dobson (1998)
PNAS 95, 7391-7395
   Abstract »    Full Text »    PDF »
Kinetic Intermediates Trapped by Native Interactions in RNA Folding.
D. K. Treiber, M. S. Rook, P. P. Zarrinkar, and J. R. Williamson (1998)
Science 279, 1943-1946
   Abstract »    Full Text »
Reconstitution of Escherichia coli RNase HI from the N-fragment with High Helicity and the C-fragment with a Disordered Structure.
E. Kanaya and S. Kanaya (1995)
J. Biol. Chem. 270, 19853-19860
   Abstract »    Full Text »    PDF »
In pursuit of protein folding.
S. Englander (1993)
Science 262, 848-849
   PDF »
Electrospray ionization mass spectrometry as a tool to analyze hydrogen/deuterium exchange kinetics of transmembrane peptides in lipid bilayers.
J. A. A. Demmers, J. Haverkamp, A. J. R. Heck, R. E. Koeppe II, and J. A. Killian (2000)
PNAS 97, 3189-3194
   Abstract »    Full Text »    PDF »


ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)