Multistep protein unfolding during nanopore translocation.
David Rodriguez-Larrea, H. Bayley
semanticscholar +3 more sources
Protein unfolding and refolding as transitions through virtual states [PDF]
Single-molecule atomic force spectroscopy probes elastic properties of titin, ubiquitin and other relevant proteins. We explain bioprotein folding dynamics under both length- and force-clamp by modeling polyprotein modules as particles in a bistable ...
Bonilla, L. L., Carpio, A., Prados, A.
core +3 more sources
Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate
ClpXP is an ATP-dependent protease in which the ClpX AAA+ motor binds, unfolds, and translocates specific protein substrates into the degradation chamber of ClpP. We present cryo-EM studies of the E.
Xue Fei +6 more
doaj +1 more source
Mechanotransduction in talin through the interaction of the R8 domain with DLC1.
The mechanical unfolding of proteins is a cellular mechanism for force transduction with potentially broad implications in cell fate. Despite this, the mechanism by which protein unfolding elicits differential downstream signalling pathways remains ...
Alexander William M Haining +7 more
doaj +1 more source
Engineering the kinetic stability of a β-trefoil protein by tuning its topological complexity
Kinetic stability, defined as the rate of protein unfolding, is central to determining the functional lifetime of proteins, both in nature and in wide-ranging medical and biotechnological applications.
Delaney M. Anderson +3 more
doaj +1 more source
Polar residues in the protein core of Escherichia coli thioredoxin are important for fold specificity [PDF]
Most globular proteins contain a core of hydrophobic residues that are inaccessible to solvent in the folded state. In general, polar residues in the core are thermodynamically unfavorable except when they are able to form intramolecular hydrogen bonds ...
Bolon, Daniel N., Mayo, Stephen L.
core +1 more source
The Effect of Dimethyl Sulfoxide on the Lysozyme Unfolding Kinetics, Thermodynamics, and Mechanism
The thermal stability of proteins in the presence of organic solvents and the search for ways to increase this stability are important topics in industrial biocatalysis and protein engineering.
Timur Magsumov +3 more
doaj +1 more source
The initial stages of protein unfolding may reflect the stability of the entire fold and can also reveal which parts of a protein can be perturbed, without restructuring the rest. In this work, we couple UVPD with activated ion mobility mass spectrometry
A. Theisen +5 more
semanticscholar +1 more source
Optimizing the calculation of energy landscape parameters from single-molecule protein unfolding experiments [PDF]
Single-molecule force spectroscopy using an atomic force microscope (AFM) can be used to measure the average unfolding force of proteins in a constant velocity experiment.
David J. Brockwell +7 more
core +1 more source
Targeted protein unfolding uncovers a Golgi-specific transcriptional stress response
In eukaryotic cells, organelle-specific stress-response mechanisms are vital for maintaining cellular homeostasis. The Golgi apparatus, an essential organelle of the secretory system, is the major site of protein modification and sorting within a cell ...
Yevgeniy V. Serebrenik +5 more
semanticscholar +1 more source

