Importance of sequence specificity for predicting protein folding pathways: Perturbed Gaussian chain model

scientific article published on November 15, 2003

Importance of sequence specificity for predicting protein folding pathways: Perturbed Gaussian chain model is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1002/PROT.10427
P953full work available at URLhttps://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fprot.10427
https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.10427
P698PubMed publication ID14579353

P2093author name stringTomoshi Kameda
P2860cites workUltrafast folding of WW domains without structured aromatic clusters in the denatured stateQ24555106
From snapshot to movie: phi analysis of protein folding transition states taken one step furtherQ24657640
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structuresQ26778412
Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solutionQ28286232
The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedureQ28306230
The SH3-fold family: experimental evidence and prediction of variations in the folding pathwaysQ30168557
Experiment and theory highlight role of native state topology in SH3 foldingQ30175284
The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved.Q30175285
A theoretical search for folding/unfolding nuclei in three-dimensional protein structuresQ30322988
A surprising simplicity to protein folding.Q30326802
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Go-ing for the prediction of protein folding mechanismsQ33750611
Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding.Q33878446
Topology, stability, sequence, and length: defining the determinants of two-state protein folding kineticsQ34031904
Spin glasses and the statistical mechanics of protein foldingQ34358450
Contact order, transition state placement and the refolding rates of single domain proteins.Q34464266
Prediction of protein-folding mechanisms from free-energy landscapes derived from native structuresQ35647310
A simple model for calculating the kinetics of protein folding from three-dimensional structuresQ35647438
How native-state topology affects the folding of dihydrofolate reductase and interleukin-1betaQ35752174
Structural correlations in protein folding funnelsQ35962279
Exploring the origins of topological frustration: design of a minimally frustrated model of fragment B of protein A.Q36543566
Theoretical Studies of Protein FoldingQ40152842
Topological and energetic factors: what determines the structural details of the transition state ensemble and "en-route" intermediates for protein folding? An investigation for small globular proteinsQ41734718
Scaling of folding properties in go models of proteinsQ42712206
Identification and characterization of the unfolding transition state of chymotrypsin inhibitor 2 by molecular dynamics simulationsQ47629807
Roles of native topology and chain-length scaling in protein folding: a simulation study with a Go-like model.Q52053541
Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading.Q52310162
"New view" of protein folding reconciled with the old through multiple unfolding simulations.Q52528318
Critical role of beta-hairpin formation in protein G folding.Q52540334
Microscopic theory of protein folding rates. I. Fine structure of the free energy profile and folding routes from a variational approachQ56688819
A breakdown of symmetry in the folding transition state of protein LQ56999420
The Structure of the Transition State for Folding of Chymotrypsin Inhibitor 2 Analysed by Protein Engineering Methods: Evidence for a Nucleation-condensation Mechanism for Protein FoldingQ57823358
Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domainQ57957112
The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBPQ58211025
Protein architecture and the origin of intronsQ68715101
The energy landscape of a fast-folding protein mapped by Ala-->Gly substitutionsQ73206090
The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topologyQ73514556
P433issue3
P407language of work or nameEnglishQ1860
P921main subjectbiochemistryQ7094
protein foldingQ847556
molecular modelQ2196961
protein secondary structureQ904984
structural biologyQ908902
P304page(s)616-628
P577publication date2003-11-01
2003-11-15
P1433published inProteinsQ7251514
P1476titleImportance of sequence specificity for predicting protein folding pathways: Perturbed Gaussian chain model
P478volume53

Reverse relations

cites work (P2860)
Q33900598Phi values in protein-folding kinetics have energetic and structural components.
Q42090681Transition states in protein folding kinetics: modeling phi-values of small beta-sheet proteins

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