Related Experiment Video
Updated: Jul 16, 2026

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
Published on: January 11, 2017
Stability of a protein tethered to a surface
Miriam Friedel1, Andrij Baumketner, Joan-Emma Shea
1Department of Physics, University of California, Santa Barbara, California 93106, USA.
Abstract:
Surface-tethered proteins are increasingly being used in a variety of experimental situations, and they are the basis for many new technologies. Nevertheless, a thorough understanding of how a surface can impact the native state stability of an attached protein is lacking. In this work, the authors use molecular dynamics simulations of a model beta-barrel protein to investigate how surface tethering influences native state stability. They find that stability, as measured by the folding temperature Tf, can be either increased, decreased, or remain unchanged as a result of tethering. Observed shifts are highly dependent on the location of residue used as the tether point, and stability is influenced by a number of factors, both energetic and entropic. These factors include native state vibrations, loss of bulk unfolded conformations, changes to the unfolded state ensemble, and the emergence of an entropic term not present for the bulk protein. They discuss each of these contributions in detail and comment on their relative importance and connection to experiment.
Related Concept Videos
Tail-anchoring of Proteins in the ER Membrane
Protein-protein Interfaces
Lipids as Anchors
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
Protein Folding
Protein Diffusion in the Membrane
Ligand Binding Sites
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

