Conspectus The function of proteins as biological nanomachines relies on their ability to fold into complex 3D structures, bind selectively to partners, and undergo conformational …
S Kim, D Lee, WCB Wijesinghe, D Min - Elife, 2023 - elifesciences.org
Single-molecule tweezers, such as magnetic tweezers, are powerful tools for probing nm- scale structural changes in single membrane proteins under force. However, the weak …
Conformational transitions of proteins are governed by chemical kinetics, often toggled by passage through an activated state separating two conformational ensembles. The passage …
C Scaletti, PPS Russell, KJ Hebel… - Proceedings of the …, 2024 - National Acad Sciences
Protein–protein and protein–water hydrogen bonding interactions play essential roles in the way a protein passes through the transition state during folding or unfolding, but the large …
S Shityakov, EV Skorb… - Royal Society Open …, 2022 - royalsocietypublishing.org
Scaling relationships for polymeric molecules establish power law dependencies between the number of molecular segments and linear dimensions, such as the radius of gyration …
The recognition of PPxY viral Late domains by the third WW domain of the human HECT-E3 ubiquitin ligase NEDD4 (NEDD4-WW3) is essential for the budding of many viruses …
The way in which multidomain proteins fold has been a puzzling question for decades. Until now, the mechanisms and functions of domain interactions involved in multidomain protein …
A Das, A Yadav, M Gupta, VL Terse… - Journal of the …, 2021 - ACS Publications
Protein-folding can go wrong in vivo and in vitro, with significant consequences for the living organism and the pharmaceutical industry, respectively. Here we propose a design principle …
N Mothi, V Muñoz - The Journal of Physical Chemistry B, 2021 - ACS Publications
The rates of protein (un) folding are often described as diffusion on the projection of a hyperdimensional energy landscape onto a few (ideally one) order parameters. Testing …