title: Towards design principles for determining the mechanical stability of proteins.
abstract: The successful integration of proteins into bionanomaterials with specific and desired functions requires an accurate understanding of their material properties. Two such important properties are their mechanical stability and malleability. While single molecule manipulation techniques now routinely provide access to these, there is a need to move towards predictive tools that can rationally identify proteins with desired material properties. We provide a comprehensive review of the available experimental data on the single molecule characterisation of proteins using the atomic force microscope. We uncover a number of empirical relationships between the measured mechanical stability of a protein and its malleability, which provide a set of simple tools that might be employed to estimate properties of previously uncharacterised proteins.
authors.affiliation: School of Physics and Astronomy, University of Leeds, Leeds, UKLS2 9JT. L.Dougan@leeds.ac.uk.
authors.forename: Toni
authors.initials: T
authors.lastname: Hoffmann
authors.forename: Katarzyna M
authors.initials: KM
authors.lastname: Tych
authors.forename: Megan L
authors.initials: ML
authors.lastname: Hughes
authors.forename: David J
authors.initials: DJ
authors.lastname: Brockwell
authors.forename: Lorna
authors.initials: L
authors.lastname: Dougan
mesh_terms: D018625:Microscopy, Atomic Force; D049329:Nanostructures / Q000737:chemistry; D011489:Protein Denaturation; D055550:Protein Stability; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D011506:Proteins