about
Protein folding funnels: a kinetic approach to the sequence-structure relationshipProtein folding: then and nowPolymer principles and protein foldingA backbone-based theory of protein foldingThe nature of protein folding pathwaysHow much of protein sequence space has been explored by life on Earth?Fragment-HMM: a new approach to protein structure predictionA simple model predicts experimental folding rates and a hub-like topologyProtein structure evaluation using an all-atom energy based empirical scoring function.Protein folding and misfolding: mechanism and principles.Splitting statistical potentials into meaningful scoring functions: testing the prediction of near-native structures from decoy conformations.Structural gymnastics of multifunctional metamorphic proteins.Principles of protein folding--a perspective from simple exact models.Protein structure prediction: challenging targets for CASP10.Local interactions and the optimization of protein folding.Reliable protein folding on complex energy landscapes: the free energy reaction pathDynamical transition and proteinquake in photoactive yellow protein.General mechanism of two-state protein folding kinetics.Energy landscape in protein folding and unfolding.Chemical, physical, and theoretical kinetics of an ultrafast folding protein.RNA folding on the 3D triangular lattice.Coordinate-dependent diffusion in protein folding.Reactive flux and folding pathways in network models of coarse-grained protein dynamics.SSC: a tool for constructing libraries for systematic screening of conformers.Simple model of protein folding kineticsExtremely slow intramolecular diffusion in unfolded protein LBehind the folding funnel diagram.Folding and finding RNA secondary structure.Computer determination of peptide conformations in water: different roads to structureConditions for the emergence of life on the early Earth: summary and reflections.Multiscale modeling of biological functions.The topomer-sampling model of protein foldingLength Dependent Helix-Coil Transition Kinetics of Nine Alanine-Based PeptidesInferring the rate-length law of protein foldingHierarchies and logarithmic oscillations in the temporal relaxation patterns of proteins and other complex systems.Elasticity, friction, and pathway of γ-subunit rotation in FoF1-ATP synthase.Hydrophobic forces and the length limit of foldable protein domainsDiscrete molecular dynamics: an efficient and versatile simulation method for fine protein characterization.Entropic barriers, transition states, funnels, and exponential protein folding kinetics: a simple modelKinetics and thermodynamics of folding in model proteins.
P2860
Q24563939-223AE58B-8DE4-45E1-89A2-DED6F94F2EE0Q24671711-F69F0A33-6DA7-4282-98EE-E759FBD7DD40Q24672635-D91C8B67-592A-49F3-BCF1-73877B36D75CQ24672727-5429077E-28CE-4F36-8F6F-F10B621143FFQ26998903-1C74F072-2F04-4FA0-9875-16C095495572Q28277287-9156D450-5733-49F0-A5A5-D7F4B799E869Q28291690-8ED238A1-9E49-47BE-8D28-A2BF859D05AEQ28728370-819A14FF-A12A-4389-8449-822D37A64673Q30352261-1FCB2D7C-D9DE-4510-B1AB-E843A76D1D4AQ30368801-83626345-B6B3-4F19-A405-BE7FCE00CD42Q30382577-A5437DAE-0318-4844-AE3F-058C38F350FBQ30402034-C3328CF0-6DA2-4604-B4FD-C195631BE0AFQ30417429-4A317090-AE1B-4CE7-8906-BFA478217A2BQ30418498-6347AE11-E45B-4D57-B1E6-816954DCC3D0Q30428832-9F1634CD-5C30-41C9-9F53-96ABE9BBC3E5Q30483310-3C89098F-C5E2-405B-A76E-DBD46063737DQ30834202-79EF4A09-7227-4B7B-861F-BB7DF09FC6F7Q30838291-7D08649C-0C7A-4315-BC47-A85349290B03Q31055077-8B016E01-0B61-468C-AD13-062645A66B29Q33387166-7D3297C5-1A96-41B4-9A5C-9C0F102CE375Q33515133-E86D883C-D5EB-4B0B-B33E-C7BF88DFE554Q33667020-D9A10F16-DE02-45D7-BAFC-EE8757181D4AQ33703260-7A294E02-F443-4DF5-BAA9-504AE2E7B293Q33859683-356C0B15-5B69-4E47-974B-7CCBEEA0822BQ33870693-1E18D7BE-C748-4755-AE23-63736F60B3A9Q34068387-C94FD71A-DB82-4C3C-B7C8-4AB6F4845999Q34193782-D898F6E3-1D23-40AC-BC18-4B4DD0FCF2B2Q34313777-6F582E1E-8435-40E7-9237-5CE7CEBB66A9Q34421284-9F58AEB9-9A00-4578-B3A6-BD46DC10C5AEQ34569774-34D60CB2-7B0D-4491-86D0-F0B748F31BA3Q35009611-E0A79385-AABB-4595-8BE6-5EF339FC98EBQ35056600-016C3E64-AF43-48FE-8B55-5E6664BE15F7Q35059469-4ACDA7A9-40F0-4547-BB59-1F32FED1A281Q35067284-66BB730A-079A-4934-8C5C-66973341C684Q35639373-30826CAA-CDC4-4AC7-9E73-C8525983692AQ36008252-2A710DF2-8E17-455C-B34E-5D4B3353EC89Q36056430-AAEF11B6-95E2-4B91-9E63-70721A956469Q36120522-FCA4AD4F-AF26-498B-B65D-4A519955C90AQ36281946-30848A73-5AA8-4C24-9B63-AA5F68D352D5Q36409017-8554E916-2A42-4B85-B513-77C6D3B80887
P2860
description
1992 nî lūn-bûn
@nan
1992 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Levinthal's paradox
@ast
Levinthal's paradox
@en
Levinthal's paradox
@nl
type
label
Levinthal's paradox
@ast
Levinthal's paradox
@en
Levinthal's paradox
@nl
prefLabel
Levinthal's paradox
@ast
Levinthal's paradox
@en
Levinthal's paradox
@nl
P2093
P356
P1476
Levinthal's paradox
@en
P2093
P2860
P356
10.1073/PNAS.89.1.20
P407
P577
1992-01-01T00:00:00Z