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Comprehensive Folding Variations for Protein Folding [PDF]

open access: yesProteins: Structure, Function, and Bioinformatics, 2022
The revelation of protein folding is a challenging subject in both discovery and description. Except acquirement of accurate 3D structure for protein stable state, another big hurdle is how to discover structural flexibility for protein innate character.
Jiaan Yang   +10 more
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Protein folds and protein folding [PDF]

open access: yesProtein Engineering Design and Selection, 2010
The classification of protein folds is necessarily based on the structural elements that distinguish domains. Classification of protein domains consists of two problems: the partition of structures into domains and the classification of domains into sets of similar structures (or folds).
R Dustin, Schaeffer, Valerie, Daggett
openaire   +2 more sources

Folding of Proteins with Diverse Folds [PDF]

open access: yesBiophysical Journal, 2006
Using parallel tempering simulations with high statistics, we investigate the folding and thermodynamic properties of three small proteins with distinct native folds: the all-helical 1RIJ, the all-sheet beta3s, and BBA5, which has a mixed helix-sheet fold.
Mohanty, S., Hansmann, U. H. E.
openaire   +3 more sources

Protein folding by NMR [PDF]

open access: yesProgress in Nuclear Magnetic Resonance Spectroscopy, 2017
Protein folding is a highly complex process proceeding through a number of disordered and partially folded nonnative states with various degrees of structural organization. These transiently and sparsely populated species on the protein folding energy landscape play crucial roles in driving folding toward the native conformation, yet some of these ...
Zhuravleva, A, Korzhnev, DM
openaire   +3 more sources

On the kinematics of protein folding [PDF]

open access: yesJournal of Computational Chemistry, 2003
AbstractWe offer simple solutions to three kinematic problems that occur in the folding of proteins. We show how to construct suitably local elementary Monte Carlo moves, how to close a loop, and how to fold a loop without breaking the bond that closes it. © 2003 Wiley Periodicals, Inc.
Sean Cahill   +2 more
openaire   +3 more sources

Protein folding [PDF]

open access: yesJournal of Cellular and Molecular Medicine, 2003
AbstractThe problem of protein folding is that how proteins acquire their native unique three‐dimensional structure in the physiological milieu. To solve the problem, the following key questions should be answered: do proteins fold co‐ or post‐translationally, i.e.
openaire   +2 more sources

The Protein Folding Network [PDF]

open access: yesJournal of Molecular Biology, 2004
The conformation space of a 20-residue antiparallel $β$-sheet peptide, sampled by molecular dynamics simulations, is mapped to a network. Conformations are nodes of the network, and the transitions between them are links. The conformation space network describes the significant free energy minima and their dynamic connectivity without projections into ...
Rao F, Caflisch A
openaire   +4 more sources

Folding nuclei in proteins [PDF]

open access: yesFEBS 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.
Galzitskaya, Oxana V   +2 more
openaire   +2 more sources

The Protein Folding Problem [PDF]

open access: yesAnnual Review of Biophysics, 2008
The “protein folding problem” consists of three closely related puzzles: (a) What is the folding code? (b) What is the folding mechanism? (c) Can we predict the native structure of a protein from its amino acid sequence? Once regarded as a grand challenge, protein folding has seen great progress in recent years.
Dill, K.   +3 more
openaire   +3 more sources

Chaos of protein folding [PDF]

open access: yesThe 2011 International Joint Conference on Neural Networks, 2011
As protein folding is a NP-complete problem, artificial intelligence tools like neural networks and genetic algorithms are used to attempt to predict the 3D shape of an amino acids sequence. Underlying these attempts, it is supposed that this folding process is predictable.
Jacques M. Bahi   +2 more
openaire   +3 more sources

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