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Detection of Transient Protein Folding Populations by Mass Spectrometry

Miranker, Andrew ; Robinson, Carol V. ; Radford, Sheena E. ; Aplin, Robin T. ; Dobson, Christopher M.

Science (American Association for the Advancement of Science), 1993-11, Vol.262 (5135), p.896-900 [Periódico revisado por pares]

Washington, DC: American Society for the Advancement of Science

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Título:
Detection of Transient Protein Folding Populations by Mass Spectrometry
Autor: Miranker, Andrew ; Robinson, Carol V. ; Radford, Sheena E. ; Aplin, Robin T. ; Dobson, Christopher M.
Assuntos: Amides ; Analytical, structural and metabolic biochemistry ; Biochemistry ; Biological and medical sciences ; Enzymes ; Fundamental and applied biological sciences. Psychology ; General aspects, investigation methods ; Hydrogen ; Hydrogen - chemistry ; Hydrogen-Ion Concentration ; Kinetics ; Magnetic Resonance Spectroscopy ; Mass spectra ; Mass Spectrometry ; Mass spectroscopy ; Models, Chemical ; Molecules ; Muramidase - chemistry ; Protein Folding ; Protein refolding ; Proteins ; Temperature ; Time constants
É parte de: Science (American Association for the Advancement of Science), 1993-11, Vol.262 (5135), p.896-900
Notas: ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
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Descrição: 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.
Editor: Washington, DC: American Society for the Advancement of Science
Idioma: Inglês

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Detection of Transient Protein Folding Populations by Mass Spectrometry

Miranker, Andrew ; Robinson, Carol V. ; Radford, Sheena E. ; Aplin, Robin T. ; Dobson, Christopher M.

Washington, DC: American Society for the Advancement of Science

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