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Journal ArticleDOI

Probing conformational changes in proteins by mass spectrometry

Swapan K. Chowdhury, +2 more
- 21 Nov 1990 - 
- Vol. 112, Iss: 24, pp 9012-9013
TLDR
The authors describe the first use of mass spectrometry for probing conformational changes in proteins in a manner analogous to that employed in techniques like optical rotary dispersion, circular dichroism, and spectrophotometry.
Abstract
Mass spectrometry has found wide application for the elucidation of the primary structures of proteins. However, with the exception of topographical studies of membrane-bound proteins, mass spectrometry has not previously been utilized to obtain information concerning in three-dimensional conformation of proteins. In the present communication, the authors describe the first use of mass spectrometry for probing conformational changes in proteins in a manner analogous to that employed in techniques like optical rotary dispersion, circular dichroism, and spectrophotometry.

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Citations
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Journal ArticleDOI

Gas-phase chemistry of the negative ions of fully-protected peptides by high-resolution electrospray ionization tandem mass spectrometry

TL;DR: The method is applied to segments of porcine calcitonin, Cal, whose [M–H]− deprotonated molecular ions provided low-energy CID mass spectra which allow the evaluation either of the primary structure of the peptide and of the location of the side-chain protective groups.
Book ChapterDOI

Mass spectrometry in proteomics

TL;DR: Peptide mapping takes advantage of the accurate mass measurement of unique protein fragments produced by highly specific enzymatic digestion to identify peptides in the size range most efficient for protein identification.
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Sulfolane-Induced Supercharging of Electrosprayed Salt Clusters: An Experimental/Computational Perspective.

TL;DR: In this paper, the authors examined how sulfolane affects electrosprayed NaI salt clusters and found that the addition of sulfoline resulted in abundant doubly charged [NanI(n-2)Sulfolane]2+ species.

FOCUS: MASS SPECTROMETRY AS A PROBE OF HIGHER ORDER PROTEIN STRUCTURE: ACCOUNT & PERSPECTIVE Revealing Higher Order Protein Structure Using Mass Spectrometry

TL;DR: A personal perspective of the increasingly useful role that mass spectrometric techniques are exerting during the elucidation of higher order protein structures and a vision for the future role of MS- based techniques in the development of a multi-scale molecular microscope is provided.
Journal ArticleDOI

Protein folding and tumour angiogenesis-do we know enough?

TL;DR: Protein folding being a highly complex and intricate phenomenon involves interesting physics and has always been an intriguing question for scientists.
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