PMID: 2110823Mar 27, 1990Paper

Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization

Biochemistry
T KiefhaberF X Schmid

Abstract

It is our aim to elucidate molecular aspects of the mechanism of protein folding. We use ribonuclease T1 as a model protein, because it is a small single-domain protein with a well-defined secondary and tertiary structure, which is stable in the presence and absence of disulfide bonds. Also, an efficient mutagenesis system is available to produce protein molecules with defined sequence variations. Here we present a preliminary characterization of the folding kinetics of ribonuclease T1. Its unfolding and refolding reactions are reversible, which is shown by the quantitative recovery of the catalytic activity after an unfolding/refolding cycle. Refolding is a complex process, where native protein is formed on three distinguishable pathways. There are 3.5% fast-folding molecules, which refold within the millisecond time range, and 96.5% slow-folding species, which regain the native state in the time range of minutes to hours. These slow-folding molecules give rise to two major, parallel refolding reactions. The mixture of fast- and slow-folding molecules is produced slowly after unfolding by chain equilibration reactions that show properties of proline isomerization. We conclude that part of the kinetic complexity of RNase T1 fol...Continue Reading

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Citations

May 1, 1992·Protein Science : a Publication of the Protein Society·R RudolphT Kiefhaber
Jul 1, 1992·Protein Science : a Publication of the Protein Society·D A SchultzR L Baldwin
Sep 1, 1992·Protein Science : a Publication of the Protein Society·T KiefhaberA Chaffotte
Feb 1, 1994·Protein Science : a Publication of the Protein Society·L M MayrF X Schmid
Jun 1, 1995·Protein Science : a Publication of the Protein Society·M H Zehfus
Jul 1, 1997·Protein Science : a Publication of the Protein Society·L S MullinsF M Raushel
Jun 1, 1992·Journal of Biotechnology·O LandtU Hahn
Dec 19, 2002·Biophysical Chemistry·Louise A Wallace, C Robert Matthews
Mar 23, 2000·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·B IshimotoS Ikawa
Jun 15, 2011·Journal of the American Chemical Society·Caroline HauptJochen Balbach
Aug 1, 1995·Nature Structural Biology·T SchindlerF X Schmid
Sep 26, 1997·Nature Structural Biology·D K HeidaryP A Jennings
May 15, 1992·Proceedings of the National Academy of Sciences of the United States of America·E R Schönbrunner, F X Schmid
Apr 26, 1994·Proceedings of the National Academy of Sciences of the United States of America·E R PriceF D McKeon
Oct 18, 2001·Protein Science : a Publication of the Protein Society·W B OuH M Zhou
Sep 7, 2000·Protein Science : a Publication of the Protein Society·T A PertinhezC M Dobson
Oct 15, 1996·European Journal of Biochemistry·T SchindlerF X Schmid
Nov 28, 2012·PloS One·Greta HultqvistPer Jemth
Jan 18, 2005·Biological Chemistry·Hisae MatsuuraKenji Takahashi
Jan 10, 2002·Journal of Molecular Biology·Louise A Wallace, C Robert Matthews
Apr 23, 2015·Proceedings of the National Academy of Sciences of the United States of America·Thuy Phuong DaoDoug Barrick
Oct 25, 2008·Fungal Genetics and Biology : FG & B·Débora PintoArnaldo Videira
Feb 1, 2008·Journal of Molecular Biology·Tobias Aumüller, Gunter Fischer
Sep 8, 2007·Journal of Molecular Biology·Benjamin T AndrewsPatricia A Jennings
May 5, 2005·The New Phytologist·Patrick RomanoSheng Luan
Jul 27, 2004·Protein Science : a Publication of the Protein Society·Yun-Ru Chen, A Clay Clark
Oct 15, 2008·Magnetic Resonance in Chemistry : MRC·Jürgen M SchmidtFrank Löhr
Jul 17, 2013·Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry·Enrico Rennella, Bernhard Brutscher
Oct 3, 2009·Protein Science : a Publication of the Protein Society·Sara L Milam, A Clay Clark

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