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Identification and characterization of protein folding intermediates
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
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2007 (English)In: Biophysical Chemistry, ISSN 0301-4622, E-ISSN 1873-4200, Vol. 128, no 2-3, 105-113 p.Article, review/survey (Refereed) Published
Abstract [en]

In order to understand the mechanism by which a polypeptide chain folds into its functionally active native state it is necessary to characterize in detail all the species accumulated along the pathway. The elusive nature of protein folding intermediates poses their identification and characterization as an extremely difficult task in the protein folding field. In the case of small single domain proteins, the direct measurement of the thermodynamics and structural parameters of protein folding intermediates has provided new insights on the nature of the forces involved in the stabilization of nascent protein structures. Here we summarize some of the experimental approaches aimed at the detection and characterization of folding intermediates along with a discussion of some general structural features emerging from these studies.

Place, publisher, year, edition, pages
2007. Vol. 128, no 2-3, 105-113 p.
Keyword [en]
Protein Folding, Proteins/*chemistry/*metabolism, Thermodynamics, Urea/chemistry
National Category
Medical and Health Sciences
URN: urn:nbn:se:uu:diva-15774DOI: 10.1016/j.bpc.2007.04.008ISI: 000247582800002PubMedID: 17498862OAI: oai:DiVA.org:uu-15774DiVA: diva2:43545
Available from: 2008-03-05 Created: 2008-03-05 Last updated: 2013-07-09Bibliographically approved

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Ivarsson, YlvaJemth, Per
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