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Folding and stability of globular proteins and implications for function
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
2009 (English)In: Current opinion in structural biology, ISSN 0959-440X, E-ISSN 1879-033X, Vol. 19, no 1, 3-7 p.Article in journal (Refereed) Published
Abstract [en]

The description of protein folding pathways and the principles that govern them has proven to be one of the most difficult problems to be solved in structural biology. But the combination of experiments and simulations has now provided a clearer picture of the chemistry involved. Once folded, however, proteins remain dynamic systems making possible both small-scale and large-scale structural and/or dynamical changes upon binding or releasing of ligands and during catalysis. In this review we focus on recent advances in the field of protein folding and discuss possible links between folding, stability, and binding dynamics.

Place, publisher, year, edition, pages
2009. Vol. 19, no 1, 3-7 p.
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Medical and Health Sciences
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URN: urn:nbn:se:uu:diva-119552DOI: 10.1016/j.sbi.2008.12.001ISI: 000264282000002PubMedID: 19157852OAI: oai:DiVA.org:uu-119552DiVA: diva2:300477
Available from: 2010-02-26 Created: 2010-02-26 Last updated: 2017-12-12Bibliographically approved

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Ivarsson, YlvaJemth, Per

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