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Folding, stability and shape of proteins in crowded environments: experimental and computational approaches
Umeå University, Faculty of Science and Technology, Chemistry.
2009 (English)In: International journal of molecular sciences, ISSN 1422-0067, Vol. 10, no 2, 572-88 p.Article in journal (Refereed) Published
Abstract [en]

How the crowded environment inside cells affects folding, stability and structures of proteins is a vital question, since most proteins are made and function inside cells. Here we describe how crowded conditions can be created in vitro and in silico and how we have used this to probe effects on protein properties. We have found that folded forms of proteins become more compact in the presence of macromolecular crowding agents; if the protein is aspherical, the shape also changes (extent dictated by native-state stability and chemical conditions). It was also discovered that the shape of the macromolecular crowding agent modulates the folding mechanism of a protein; in addition, the extent of asphericity of the protein itself is an important factor in defining its folding speed.

Place, publisher, year, edition, pages
2009. Vol. 10, no 2, 572-88 p.
Keyword [en]
Macromolecular crowding, Ficoll® 70, energy landscape theory, off-lattice model, excluded volume effect, protein folding mechanism, spectroscopy
Identifiers
URN: urn:nbn:se:umu:diva-22142DOI: 10.3390/ijms10020572PubMedID: 19333422OAI: oai:DiVA.org:umu-22142DiVA: diva2:212852
Available from: 2009-04-24 Created: 2009-04-24 Last updated: 2010-01-12Bibliographically approved

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Wittung-Stafshede, Pernilla

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