Work

Folding, Stability and Shape of Proteins in Crowded Environments: Experimental and Computational Approaches

Year: 2009

Type: review

Abstract: 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.

Source: International Journal of Molecular Sciences

DOI: 10.3390/ijms10020572

Authors: Antonios Samiotakis, Pernilla Wittung-Stafshede, Margaret S. Cheung

Institutions: University of Houston, Umeå University

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $3,499

Funders: Welch Foundation, Umeå Universitet, Texas Center for Superconductivity, University of Houston