Protein folding monitored at individual residues during a two- dimensional NMR experiment

Science

Volumn 274, Issue 5290, 1996, Pages 1161-1163

  Balbach, Jochen ^a,c   Forge, Vincent ^a,d   Lau, Wai Shun ^a   Van Nuland, Nico A J ^a   Brew, Keith ^b   Dobson, Christopher M ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF MIAMI MILLER SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF BAYREUTH   (Germany)

^d DIF   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA LACTALBUMIN; NITROGEN 15;

ARTICLE; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTEIN SYNTHESIS;

CIRCULAR DICHROISM; FOURIER ANALYSIS; HYDROGEN-ION CONCENTRATION; KINETICS; LACTALBUMIN; MAGNETIC RESONANCE SPECTROSCOPY; NITROGEN ISOTOPES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE;

ALOCASIA MACRORRHIZOS; BOVINAE;

EID: 0029860435     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.274.5290.1161     Document Type: Article

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47. We thank S. L. Winder and P. J. Hore for help in developing the rapid mixing device. J.B., V.F., and N.A.J.v.N. were supported by the Human Capital and Mobility Programme of the European Community. K.B. is supported by a grant from NIH. The Oxford Centre for Molecular Sciences is supported by the Engineering and Physical Sciences Research Council, Biotechnology and Biological Sciences Research Council, and Medical Research Council (UK). C.M.D. is supported in part by an International Research Scholars award from the Howard Hughes Medical Institute.