Results 61 to 70 of about 6,757,592 (330)
Targeting of client proteins to the VCP/p97/Cdc48 unfolding machine
Frontiers in Molecular Biosciences, 2023 The AAA+ ATPase p97 (also called VCP or Cdc48) is a major protein unfolding machine with hundreds of clients in diverse cellular pathways that are critical for cell homeostasis, proliferation and signaling. In this review, we summarize recent advances in
Hemmo Meyer, Johannes van den Boom
doaj +1 more source
Protein unfolding mechanisms and their effects on folding experiments
F1000Research, 2017 In this review, I discuss the various methods researchers use to unfold proteins in the lab in order to understand protein folding both in vitro and in vivo. The four main techniques, chemical-, heat-, pressure- and force-denaturation, produce distinctly
Lisa J. Lapidus
semanticscholar +1 more source
The role of a disulfide bridge in the stability and folding kinetics of Arabidopsis thaliana cytochrome c6A [PDF]
, 2011 Cytochrome c 6A is a eukaryotic member of the Class I cytochrome c family possessing a high structural homology with photosynthetic cytochrome c 6 from cyanobacteria, but structurally and functionally distinct through the presence of a disulfide bond and
Arslan +64 more
core +1 more source
Quarterly Reviews of Biophysics (print), 2016 Thermally-induced protein unfolding is commonly described with the two-state model. This model assumes only two types of protein molecules in solution, the native (N) and the denatured, unfolded (U) protein.
J. Seelig, H. Schönfeld
semanticscholar +1 more source
In‐depth interrogation of protein thermal unfolding data with MoltenProt
Protein Science, 2020 Protein stability is a key factor in successful structural and biochemical research. However, the approaches for systematic comparison of protein stability are limited by sample consumption or compatibility with sample buffer components. Here we describe
V. Kotov +13 more
semanticscholar +1 more source
Force-dependent switch in protein unfolding pathways and transition-state movements [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 2015 Significance Single-domain proteins with symmetrical arrangement of secondary structural elements in the native state are expected to fold by diverse pathways.
Pavel I Zhuravlev +4 more
semanticscholar +1 more source
Stretching of proteins in a uniform flow
, 2006 Stretching of a protein by a fluid flow is compared to that in a force-clamp apparatus. The comparison is made within a simple topology-based dynamical model of a protein in which the effects of the flow are implemented using Langevin dynamics.
Chan E. Y., Marek Cieplak, P. Szymczak
core +1 more source
Protein mechanical unfolding: a model with binary variables
, 2007 A simple lattice model, recently introduced as a generalization of the Wako--Sait\^o model of protein folding, is used to investigate the properties of widely studied molecules under external forces.
Imparato, A., Pelizzola, A., Zamparo, M.
core +1 more source
Weak and saturable protein-surfactant interactions in the denaturation of apo-α-lactalbumin by acidic and lactonic sophorolipid [PDF]
, 2016 Biosurfactants are of growing interest as sustainable alternatives to fossil-fuel-derived chemical surfactants, particularly for the detergent industry.
Brian Stougaard Vad +5 more
core +2 more sources
Calpain small subunit homodimerization is robust and calcium‐independent
FEBS Letters, EarlyView.Calpains dimerize via penta‐EF‐hand (PEF) domains. Using single‐molecule force spectroscopy, we measured the strength and kinetics of PEF–PEF homodimer binding. The interaction is robust, shows a transient conformational step before dissociation, and remains largely insensitive to Ca2+.
Nesha May O. Andoy +4 more
wiley +1 more source