Results 371 to 380 of about 6,828,531 (409)

Complexity of protein folding

Bulletin of Mathematical Biology, 1993
It is believed that the native folded three-dimensional conformation of a protein is its lowest free energy state, or one of its lowest. It is shown here that both a two- and three-dimensional mathematical model describing the folding process as a free energy minimization problem is NP-hard.
openaire   +2 more sources

Protein Folding | Protein Folding and Assembly

Encyclopedia of Biological Chemistry III, 2021
D. Goldenberg
semanticscholar   +1 more source

Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons

Proteins: Structure, Function, and Bioinformatics, 1991
A. Nicholls, K. Sharp, B. Honig
semanticscholar   +1 more source

Protein folding and misfolding

Nature, 2003
C. Dobson
semanticscholar   +1 more source

Molecular chaperones in protein folding and proteostasis

Nature, 2011
F. Hartl, A. Bracher, M. Hayer-Hartl
semanticscholar   +1 more source

…but not to protein folding?

Nature Medicine, 1995
Danuta Plochocka, Andrezj Kierzek, Plotr Zlelenkiewicz   +2 more
openaire   +3 more sources

Is protein folding rate dependent on number of folding stages? Modeling of protein folding with ferredoxin-like fold

Biochemistry (Moscow), 2010
Statistical analysis of protein folding rates has been done for 84 proteins with available experimental data. A surprising result is that the proteins with multi-state kinetics from the size range of 50-100 amino acid residues (a.a.) fold as fast as proteins with two-state kinetics from the same size range. At the same time, the proteins with two-state
openaire   +3 more sources

Protein folding in the cell

Nature, 1992
M. Gething, J. Sambrook
semanticscholar   +1 more source

Folding proteins

Nature, 1990
N J, Darby, T E, Creighton
openaire   +2 more sources

Molecular chaperones in cellular protein folding

Nature, 1996
F. Hartl
semanticscholar   +1 more source