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- Title
Analyzing protein functions in four dimensions.
- Authors
Hajdu, J; Neutze, R; Sjögren, T; Edman, K; Szöke, A; Wilmouth, R C; Wilmot, C M
- Abstract
Time-resolved structural studies on biomolecular function are coming of age. Focus has shifted from studies on 'systems of opportunities' to a more problem-oriented approach, addressing significant questions in biology and chemistry. An important step in this direction has been the use of physical and chemical trapping methods to capture and then freeze reaction intermediates in crystals. Subsequent monochromatic data collection at cryogenic temperatures can produce high resolution structures of otherwise elusive intermediates. The combination of diffraction methods with spectroscopic techniques provides a means to directly correlate electronic transitions with structural transitions in the sample, eliminating much of the guesswork from experiments. Studies on cytochrome P450, isopenicillin N synthase, cytochrome cd1 nitrite reductase, copper amine oxidase and bacteriorhodopsin were selected as examples, and the results are discussed.
- Publication
Nature structural biology, 2000, Vol 7, Issue 11, p1006
- ISSN
1072-8368
- Publication type
Journal Article
- DOI
10.1038/80911