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Protein folding: Vexing debates on a fundamental problem
Univ Rome, Ist Pasteur, Fdn Cenci Bolognetti, I-00185 Rome, Italy.;Univ Rome, Dipartimento Sci Biochim A Rossi Fanelli Sapienza, Ist Biol & Patol Mol, CNR, I-00185 Rome, Italy.;Univ Cambridge, Dept Chem, Lensfield Rd, Cambridge CB2 1EW, England..
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
2016 (English)In: Biophysical Chemistry, ISSN 0301-4622, E-ISSN 1873-4200, Vol. 212, 17-21 p.Article, review/survey (Refereed) Published
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Text
Abstract [en]

The folding of proteins has been at the heart of protein chemistry and biophysics ever since the pioneering experiments by the labs of Fred Richards and Christian Anfinsen. But, despite nearly 60 years of intense research, there are unresolved issues and a lively debate regarding some aspects of this fundamental problem. In this review we give a personal account on some key topics in the field: (i) the nature of the denatured state of a protein, (ii) nucleation sites in the folding reaction, and (iii) the time it takes for individual molecules to traverse the transition state.

Place, publisher, year, edition, pages
2016. Vol. 212, 17-21 p.
Keyword [en]
Protein folding, Kinetics, Mutagenesis, Denatured state, Transition state, Transition path time
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
URN: urn:nbn:se:uu:diva-299179DOI: 10.1016/j.bpc.2016.03.001ISI: 000374625600003PubMedID: 27018826OAI: oai:DiVA.org:uu-299179DiVA: diva2:949054
Funder
Swedish Research Council, 2012- 5096
Available from: 2016-07-15 Created: 2016-07-15 Last updated: 2016-07-15Bibliographically approved

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