Analyzing protein functions in four dimensions

Janos Hajdu, Richard Neutze, Tove Sjögren, Karl Edman, Abraham Szöke, Rupert C. Wilmouth, Carrie M. Wilmot

Research output: Contribution to journalReview articlepeer-review

60 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1006-1012
Number of pages7
JournalNature Structural Biology
Volume7
Issue number11
DOIs
StatePublished - 2000

Bibliographical note

Funding Information:
This work was supported by the Swedish Research Councils, the EU-Biotech Programme STINT, EMBO and the BBSRC Structural Biology Initiative.

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