Results 51 to 60 of about 6,813,928 (408)

Multiple Folding Pathways of the SH3 domain [PDF]

, 2003
Experimental observations suggest that proteins follow different pathways under different environmental conditions. We perform molecular dynamics simulations of a model of the SH3 domain over a broad range of temperatures, and identify distinct pathways ...
Abkevich, Alder, Bachmann, Berman, Borreguero, Branden, Bryngelson, Capaldi, Cheung, Choe, Clementi, Ding, Dokholyan, Dokholyan, Eaton, England, Feng Ding, Ferguson, Fersht, Fersht, Fersht, Fersht, Filimonov, García, Gnanakaran, Gorski, Grantcharova, Grantcharova, Guerois, Gutin, Gō, H. Eugene Stanley, Heidary, Holm, Ikai, Isaacson, Jackson, Jose M. Borreguero, Juneja, Kamagata, Karanicolas, Karplus, Khorasanizadeh, Kiefhaber, Kitahara, Klimov, Knapp, Kortemme, Lopez-Hernandez, Luque, Martinez, Matouschek, Millet, Mirny, Nikolay V. Dokholyan, Northey, Otzen, Ozkan, Paci, Pande, Plaxco, Plaxco, Plotkin, Rapaport, Riddle, Sanchez, Sergey V. Buldyrev, Shea, Shortle, Silverman, Simmons, Socci, Tang, Thirumalai, Tiana, Viguera, Viguera, Villegas, Walkenhorst, Wu, Yamasaki, Zagrovic, Zhou, Zhou   +83 more
core   +5 more sources

Deposition pattern and subcellular distribution of disease-associated prion protein in cerebellar organotypic slice cultures infected with scrapie

Frontiers in Neuroscience, 2015
Organotypic cerebellar slices represent a suitable model for characterizing and manipulating prion replication in complex cell environments. Organotypic slices recapitulate prion pathology and are amenable to drug testing in the absence of a blood-brain ...
Hanna eWolf, Andre eHossinger, Andrea eFehlinger, Sven eBuettner, Valerie eSim, Debbie eMcKenzie, Ina Maja Vorberg, Ina Maja Vorberg   +7 more
doaj   +1 more source

In silico evidence that protein unfolding is as a precursor of the protein aggregation [PDF]

ChemPhysChem 2020, 21, 377, 2019
We present a computational study on the folding and aggregation of proteins in aqueous environment, as function of its concentration. We show how the increase of the concentration of individual protein species can induce a partial unfolding of the native conformation without the occurrence of aggregates. A further increment of the protein concentration
arxiv   +1 more source

Microsecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump [PDF]

, 2004
The small size (58 residues) and simple structure of the B domain of staphylococcal protein A (BdpA) have led to this domain being a paradigm for theoretical studies of folding.
A. Drysdale, Alonso, Aronsson, Ballew, Berriz, Bieri, Boczko, Crane, D. A. Smith, Fersht, G. Dimitriadis, Galzitskaya, Guo, Hagen, Huang, Islam, J. K. Myers, Jackson, Jewett, Kragelund, Kubelka, Lapidus, Mayor, Myers, P. Arora, Plaxco, S. E. Radford, Santoro, Schindler, Schuler, Skolnick, Snow, T. G. Oas, Villegas, Wolynes, Yang, Yeh, Zhou   +37 more
core   +2 more sources

PROTEIN FOLDING AND HETEROPOLYMERS [PDF]

, 1997
57 pages, 7 figures. Uses lprocl.sty (included). To appear in " Spin glasses and random fields ", A.P.
Garel, Thomas, Orland, Henri, Pitard, Estelle   +2 more
openaire   +4 more sources

Identifying the protein folding nucleus using molecular dynamics [PDF]

, 2000
Molecular dynamics simulations of folding in an off-lattice protein model reveal a nucleation scenario, in which a few well-defined contacts are formed with high probability in the transition state ensemble of conformations.
Buldyrev, Sergey V., Dokholyan, Nikolay V., Shakhnovich, Eugene I., Stanley, Harry E.   +3 more
core   +1 more source

Secondary Forces in Protein Folding.

ACS Chemical Biology, 2019
A complete inventory of the forces governing protein folding is critical for productive protein modeling, including structure prediction and de novo design, as well as understanding protein misfolding diseases of clinical significance.
R. Newberry, Ronald T. Raines
semanticscholar   +1 more source

Simulations of protein folding [PDF]

Nuclear Physics B - Proceedings Supplements, 2000
LATTICE99(Theoretical Developments), 3 pages, latex; new version has better ...
Mark E. Fleharty, Kevin Cahill, Michael Cahill   +2 more
openaire   +3 more sources

Folding nuclei in proteins [PDF]

FEBS Letters, 2001
When a protein folds or unfolds, it passes through many half‐folded microstates. Only a few of them can accumulate and be seen experimentally, and this happens only when the folding (or unfolding) occurs far from the point of thermodynamic equilibrium between the native and denatured states.
Alexei V. Finkelstein, Dmitry N. Ivankov, Oxana V. Galzitskaya   +2 more
openaire   +4 more sources

The Structure of Human Prions: From Biology to Structural Models—Considerations and Pitfalls

Viruses, 2014
The Structure of Human Prions: From Biology to Structural Models — Considerations and ...
Claudia Y. Acevedo-Morantes, Holger Wille   +1 more
doaj   +1 more source