Molecular Hinges in Protein Folding:  the Urea-Denatured State of Apomyoglobin†

Stephan Schwarzinger; Peter E. Wright; H. Jane Dyson

doi:10.1021/bi020381o

journal article Sep 25, 2002

Molecular Hinges in Protein Folding: the Urea-Denatured State of Apomyoglobin†

Stephan Schwarzinger Peter E. Wright

H. Jane Dyson

Biochemistry Vol. 41 No. 42 pp. 12681-12686 · American Chemical Society (ACS)

View at Publisher Save 10.1021/bi020381o

Topics

No keywords indexed for this article. Browse by subject →

References

45

[1]

Jennings P. A. (1993)

[2]

Eliezer D. (2000)

[3]

Yao J. (2001)

[4]

Eliezer D. (1998)

[5]

Jennings P. A. J. Biomol. NMR (1995) 10.1007/bf00197808

[6]

Van Geet A. L. (1970)

[7]

Yao J. FEBS Lett. (1997)

[8]

Muhandiram D. R. J. Magn. Reson., B (1994) 10.1006/jmrb.1994.1032

[9]

Löhr F. J. Biomol. NMR (1995) 10.1007/bf00211783

[10]

Wittekind M. J. Magn. Reson. (1993)

[11]

Grzesiek S. J. Am. Chem. Soc. (1992) 10.1021/ja00042a003

[12]

Zhang O. J. Biomol. NMR (1994) 10.1007/bf00398413

[13]

Delaglio F. J. Biomol. NMR (1995) 10.1007/bf00197809

[14]

Johnson B. A. J. Chem. Phys. (1994)

[15]

Farrow N. A. (1994)

[16]

Viles J. H. J. Biomol. NMR (2001) 10.1023/a:1011966718826

[17]

Farrow N. A. J. Biomol. NMR (1995) 10.1007/bf00211779

[18]

Rose G. D. (1985)

[19]

Kyte J. J. Mol. Biol. (1982) 10.1016/0022-2836(82)90515-0

[20]

Gaboriaud C. FEBS Lett. (1987) 10.1016/0014-5793(87)80439-8

[21]

Thompson J. D. (1994)

[22]

Schwarzinger S. J. Biomol. NMR (2000) 10.1023/a:1008386816521

[23]

Schwarzinger S. J. Am. Chem. Soc. (2001) 10.1021/ja003760i

[24]

Schwalbe H. (1997)

[25]

Zhang O. (1995)

[26]

Meekhof A. E. J. Mol. Biol. (1999) 10.1006/jmbi.1998.2479

[27]

Frank M. K. (1995)

[28]

Geierstanger B. (1998)

[29]

Schiffer C. A. (1996)

[30]

Jorgensen W. L. Philos. Trans. R. Soc. London, Ser. A (1993)

[31]

Dötsch V. FEBS Lett. (1995) 10.1016/0014-5793(95)00459-m

[32]

Liepinsh E. J. Am. Chem. Soc. (1994) 10.1021/ja00100a036

[33]

Graziano G. J. Phys. Chem. B (2001)

[34]

Hu Y. J. Chem. Phys. (1990)

[35]

Farrow N. A. (1997)

[36]

Buck M. J. Mol. Biol. (1996) 10.1006/jmbi.1996.0193

[37]

Penkett C. J. (1998)

[38]

A simplified representation of protein conformations for rapid simulation of protein folding

Michael Levitt

Journal of Molecular Biology 1976 10.1016/0022-2836(76)90004-8

[39]

Klein-Seetharaman J. (2002)

[40]

Lipari G. J. Am. Chem. Soc. (1982)

[41]

Lipari G. J. Am. Chem. Soc. (1982)

[42]

Lietzow M. A. J. Mol. Biol. (2002) 10.1016/s0022-2836(02)00847-1

[43]

Neri D. (1992)

[44]

Fong S. J. Mol. Biol. (1998) 10.1006/jmbi.1998.1702

[45]

Abbreviations NMR

Cited By

114

Towards a robust description of intrinsic protein disorder using nuclear magnetic resonance spectroscopy

Robert Schneider, Jie-rong Huang · 2011

Molecular BioSystems

Structure and Disorder in an Unfolded State under Nondenaturing Conditions from Ensemble Models Consistent with a Large Number of Experimental Restraints

Joseph A. Marsh, Julie D. Forman-Kay · 2009

Journal of Molecular Biology

Detailed Structural Characterization of Unbound Protein Phosphatase 1 Inhibitors

Barbara Dancheck, Angus C. Nairn · 2008

Biochemistry

Detection of initiation sites in protein folding of the four helix bundle ACBP by chemical shift analysis

Kristofer Modig, Vibeke W. Jürgensen · 2007

FEBS Letters

Motional properties of unfolded ubiquitin: a model for a random coil protein

Julia Wirmer, Wolfgang Peti · 2006

Journal of Biomolecular NMR

Toward an Accurate Theoretical Framework for Describing Ensembles for Proteins under Strongly Denaturing Conditions

Hoang T. Tran, Rohit V. Pappu · 2006

Biophysical Journal

Fast Time Scale Dynamics of Protein Backbones: NMR Relaxation Methods, Applications, and Functional Consequences

Virginia A. Jarymowycz, Martin J. Stone · 2006

Chemical Reviews

Dynamics in the Unfolded State of β2-microglobulin Studied by NMR

Geoffrey W. Platt, Victoria J. McParland · 2005

Journal of Molecular Biology

Elucidation of the Protein Folding Landscape by NMR

H.Jane Dyson, Peter E. Wright · 2005

Methods in Enzymology

Folding Regulates Autoprocessing of HIV-1 Protease Precursor

Amarnath Chatterjee, P. Mridula · 2005

Journal of Biological Chemistry

Unfolded Proteins and Protein Folding Studied by NMR

H. Jane Dyson, Peter E. Wright · 2004

Chemical Reviews

NMR Characterization of the Dynamics of Biomacromolecules

Arthur G. Palmer · 2004

Chemical Reviews

Combining prediction, computation and experiment for the characterization of protein disorder

Clay Bracken, Lilia M Iakoucheva · 2004

Current Opinion in Structural Biolo...

Mapping Long-range Contacts in a Highly Unfolded Protein

Michael A. Lietzow, Marc Jamin · 2002

Journal of Molecular Biology

Metrics

114

Citations

45

References

Details

Published: Sep 25, 2002
Vol/Issue: 41(42)
Pages: 12681-12686

Authors

S

Stephan Schwarzinger

Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037

P

Peter E. Wright

Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037

H

H. Jane Dyson

Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037

Cite This Article

Stephan Schwarzinger, Peter E. Wright, H. Jane Dyson (2002). Molecular Hinges in Protein Folding: the Urea-Denatured State of Apomyoglobin†. Biochemistry, 41(42), 12681-12686. https://doi.org/10.1021/bi020381o

Molecular Hinges in Protein Folding: the Urea-Denatured State of Apomyoglobin†

You May Also Like