Biomolecules under mechanical force

S Kumar, MS Li - Physics Reports, 2010 - Elsevier
Recent advances in single molecule experiments have raised many challenges. These
challenges can be met by a proper understanding of the inter-and intra-molecular …

[HTML][HTML] The Wako-Saitô-Muñoz-Eaton model for predicting protein folding and dynamics

K Ooka, R Liu, M Arai - Molecules, 2022 - mdpi.com
Despite the recent advances in the prediction of protein structures by deep neutral networks,
the elucidation of protein-folding mechanisms remains challenging. A promising theory for …

Mapping the topography of a protein energy landscape

RD Hutton, J Wilkinson, M Faccin… - Journal of the …, 2015 - ACS Publications
Protein energy landscapes are highly complex, yet the vast majority of states within them
tend to be invisible to experimentalists. Here, using site-directed mutagenesis and exploiting …

Reconstructing the free-energy landscape of a polyprotein by single-molecule experiments

A Imparato, F Sbrana, M Vassalli - Europhysics Letters, 2008 - iopscience.iop.org
The mechanical unfolding of an engineered protein composed of eight domains of Ig27 is
investigated by using atomic force microscopy. Exploiting a fluctuation relation, the …

[HTML][HTML] Changing the mechanical unfolding pathway of FnIII10 by tuning the pulling strength

S Mitternacht, S Luccioli, A Torcini, A Imparato… - Biophysical …, 2009 - cell.com
We investigate the mechanical unfolding of the tenth type III domain from fibronectin (FnIII
10) both at constant force and at constant pulling velocity, by all-atom Monte Carlo …

Mechanical unfolding and refolding pathways of ubiquitin

A Imparato, A Pelizzola - Physical review letters, 2008 - APS
Mechanical unfolding and refolding of ubiquitin are studied by Monte Carlo simulations of a
Gō model with binary variables. The exponential dependence of the time constants on the …

Observing the osmophobic effect in action at the single molecule level

D Aioanei, I Tessari, L Bubacco… - Proteins: Structure …, 2011 - Wiley Online Library
Protecting osmolytes are widespread small organic molecules able to stabilize the folded
state of most proteins against various denaturing stresses in vivo. The osmophobic model …

[HTML][HTML] Worm-like Ising model for protein mechanical unfolding under the effect of osmolytes

D Aioanei, M Brucale, I Tessari, L Bubacco, B Samorì - Biophysical journal, 2012 - cell.com
We show via single-molecule mechanical unfolding experiments that the osmolyte glycerol
stabilizes the native state of the human cardiac I27 titin module against unfolding without …

Effects of confinement on thermal stability and folding kinetics in a simple Ising-like model

M Caraglio, A Pelizzola - Physical biology, 2012 - iopscience.iop.org
In a cellular environment, confinement and macromolecular crowding play an important role
in thermal stability and folding kinetics of a protein. We have resorted to a generalized …

Analysis of the equilibrium and kinetics of the ankyrin repeat protein myotrophin

M Faccin, P Bruscolini, A Pelizzola - The Journal of chemical physics, 2011 - pubs.aip.org
We apply the Wako-Saito-Muñoz-Eaton model to the study of myotrophin, a small ankyrin
repeat protein, whose folding equilibrium and kinetics have been recently characterized …