Special Issue "Protein Folding"

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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry, Molecular Biology and Biophysics".

Deadline for manuscript submissions: closed (31 January 2009)

Special Issue Editors

Guest Editor
Dr. Andrei Alexandrescu
Molecular & Cell Biology, University of Connecticut, BSP 209, 91 North Eagleville Road, Unit 3125, Storrs, CT 06269-3125, USA
Website: http://mcb.uconn.edu/fac.php?name=alexandrescuat
E-Mail: andrei@uconn.edu
Phone: +1 860 486 4414
Fax: +1 860 486 4331
Interests: protein folding; amyloids; alzheimer\'s disease; parkinson\'s disease; type II diabetes; structural biology; nuclear magnetic resonance spectroscopy; structural bioinformatics; protein misfolding; neuromuscular junction proteins; OB-fold proteins; protein dynamics; biophysics

Editorial Advisor
Prof. Dr. Martin Gruebele
Department of Chemistry, University of Illinois, A220 Chemical & Life Sciences Lab, 600 South Mathews Avenue, Urbana, IL 61801, USA
Website: http://www.scs.uiuc.edu/chem/faculty/Martin_Gruebele.html
E-Mail: gruebele@scs.uiuc.edu
Phone: +1 217 333 1624
Fax: +1 217 244 3186
Interests: protein folding; RNA folding; downhill folding; protein-protein interactions; biomolecular simulation; temperature jump; small angle X-ray scattering

Special Issue Information

Dear Colleagues,

In recent years protein folding often seems to have become synonymous with protein structure prediction. The field of protein folding is in fact considerably more encompassing than the ability to stitch together recurrent structural motifs into models that come closer to a target than those of competitors. The targets are moving, and as predictions become more sophisticated with each passing tournament, so does our appreciation of the intricacies of protein structure, function, and dynamics.

The papers in this issue highlight work at the frontiers of protein folding research. Topics include the behaviors of proteins under extreme or non-physiological environments such as the interactions of proteins with surfaces, synthetic matrices, chaotropes and kosmotropes, and the sheltering environment of chaperones. The mechanisms by which protein misfolding leads to disease remains a challenging and medically important problem. New experimental approaches and new ways of thinking about protein folding are described. And finally, there are papers that continue to address the fundamental unresolved problem of how protein sequences encode for the three-dimensional structures of proteins.

In a climate that often emphasizes the "biology" bottom line, it is refreshing to see basic science flourishing and needed as much as ever in research that may not translate to a pharmaceutical pill but that has and will continue to reveal fundamental insights into the roles of molecular structures in health and disease. Yes, protein folding has been "solved" many times over but it keeps presenting interesting problems and opportunities that should continue to challenge the most ambitious investigators for years to come.

Andrei Alexandrescu
Guest Editor

Related Special Issues

Protein Folding 2011 in IJMS

Keywords

  • folding and docking/binding
  • protein misfolding
  • protein folding and transient aggregation
  • MD simulation of folding
  • folding heterogeneity and intermediates
  • energy landscapes, analysis
  • energy landscapes, computation
  • dynamics and kinetics, experiments
  • single molecule folding, spectroscopy
  • single molecule folding, force
  • elementary reactions, secondary structure
  • downhill folding
  • calorimetric folding/unfolding
  • protein folding and design
  • protein folding and evolution
  • protein dynamics computation, vibrational dynamics
  • chaperoning and in vivo folding
  • transition state analysis
  • crowding and folding

Published Papers (25 papers)

Int. J. Mol. Sci. 2009, 10(6), 2838-2848; doi:10.3390/ijms10062838
Received: 26 May 2009; in revised form: 18 June 2009 / Accepted: 19 June 2009 / Published: 22 June 2009
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Int. J. Mol. Sci. 2009, 10(5), 2412-2430; doi:10.3390/ijms10052412
Received: 1 April 2009; in revised form: 16 May 2009 / Accepted: 19 May 2009 / Published: 22 May 2009
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Int. J. Mol. Sci. 2009, 10(5), 2066-2083; doi:10.3390/ijms10052066
Received: 27 April 2009; in revised form: 8 May 2009 / Accepted: 11 May 2009 / Published: 12 May 2009
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Int. J. Mol. Sci. 2009, 10(5), 2041-2053; doi:10.3390/ijms10052041
Received: 14 March 2009; in revised form: 11 April 2009 / Accepted: 14 April 2009 / Published: 6 May 2009
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Int. J. Mol. Sci. 2009, 10(4), 1808-1823; doi:10.3390/ijms10041808
Received: 14 January 2009; in revised form: 30 March 2009 / Accepted: 7 April 2009 / Published: 21 April 2009
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Int. J. Mol. Sci. 2009, 10(4), 1552-1566; doi:10.3390/ijms10041552
Received: 11 February 2009; in revised form: 20 March 2009 / Accepted: 31 March 2009 / Published: 8 April 2009
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Int. J. Mol. Sci. 2009, 10(4), 1567-1589; doi:10.3390/ijms10041567
Received: 30 January 2009; in revised form: 30 March 2009 / Accepted: 2 April 2009 / Published: 8 April 2009
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Int. J. Mol. Sci. 2009, 10(4), 1476-1499; doi:10.3390/ijms10041476
Received: 26 February 2009; in revised form: 27 March 2009 / Accepted: 30 March 2009 / Published: 1 April 2009
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Int. J. Mol. Sci. 2009, 10(3), 1369-1385; doi:10.3390/ijms10031369
Received: 28 January 2009; in revised form: 19 March 2009 / Accepted: 23 March 2009 / Published: 24 March 2009
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Int. J. Mol. Sci. 2009, 10(3), 1346-1359; doi:10.3390/ijms10031346
Received: 3 February 2009; in revised form: 8 March 2009 / Accepted: 17 March 2009 / Published: 20 March 2009
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Int. J. Mol. Sci. 2009, 10(3), 1360-1368; doi:10.3390/ijms10031360
Received: 19 February 2009; in revised form: 13 March 2009 / Accepted: 17 March 2009 / Published: 20 March 2009
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Int. J. Mol. Sci. 2009, 10(3), 1314-1345; doi:10.3390/ijms10031314
Received: 30 January 2009; in revised form: 13 March 2009 / Accepted: 18 March 2009 / Published: 19 March 2009
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Int. J. Mol. Sci. 2009, 10(3), 1121-1137; doi:10.3390/ijms10031121
Received: 2 February 2009; in revised form: 5 March 2009 / Accepted: 9 March 2009 / Published: 12 March 2009
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Int. J. Mol. Sci. 2009, 10(3), 1064-1080; doi:10.3390/ijms10031064
Received: 26 January 2009; in revised form: 6 March 2009 / Accepted: 10 March 2009 / Published: 11 March 2009
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Int. J. Mol. Sci. 2009, 10(3), 1013-1030; doi:10.3390/ijms10031013
Received: 15 January 2009; in revised form: 4 March 2009 / Accepted: 9 March 2009 / Published: 10 March 2009
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Int. J. Mol. Sci. 2009, 10(3), 817-834; doi:10.3390/ijms10030817
Received: 5 February 2009; in revised form: 23 February 2009 / Accepted: 24 February 2009 / Published: 2 March 2009
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Int. J. Mol. Sci. 2009, 10(3), 844-861; doi:10.3390/ijms10030844
Received: 9 February 2009; in revised form: 23 February 2009 / Accepted: 26 February 2009 / Published: 2 March 2009
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Int. J. Mol. Sci. 2009, 10(3), 889-905; doi:10.3390/ijms10030889
Received: 21 January 2009; in revised form: 23 February 2009 / Accepted: 26 February 2009 / Published: 2 March 2009
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Int. J. Mol. Sci. 2009, 10(3), 906-928; doi:10.3390/ijms10030906
Received: 11 January 2009; Accepted: 23 February 2009 / Published: 2 March 2009
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Int. J. Mol. Sci. 2009, 10(2), 646-655; doi:10.3390/ijms10020646
Received: 18 January 2009; in revised form: 1 February 2009 / Accepted: 10 February 2009 / Published: 20 February 2009
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Int. J. Mol. Sci. 2009, 10(2), 616-628; doi:10.3390/ijms10020616
Received: 31 October 2008; in revised form: 15 February 2009 / Accepted: 17 February 2009 / Published: 18 February 2009
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Int. J. Mol. Sci. 2009, 10(2), 572-588; doi:10.3390/ijms10020572
Received: 11 December 2008; in revised form: 10 February 2009 / Accepted: 12 February 2009 / Published: 13 February 2009
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Int. J. Mol. Sci. 2008, 9(12), 2515-2542; doi:10.3390/ijms9122515
Received: 6 November 2008; in revised form: 3 December 2008 / Accepted: 8 December 2008 / Published: 10 December 2008
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Int. J. Mol. Sci. 2008, 9(12), 2424-2446; doi:10.3390/ijms9122424
Received: 18 August 2008; in revised form: 24 November 2008 / Accepted: 2 December 2008 / Published: 3 December 2008
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Int. J. Mol. Sci. 2008, 9(9), 1753-1771; doi:10.3390/ijms9091753
Received: 13 August 2008; in revised form: 3 September 2008 / Accepted: 13 September 2008 / Published: 16 September 2008
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Last update: 26 February 2014

Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert