about
Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequencesBiomolecular electrostatics and solvation: a computational perspectiveThe dynamic conformational cycle of the group I chaperonin C-termini revealed via molecular dynamics simulationThe protein folding problemFunctional assembly of protein fragments induced by spatial confinementAb initio H2O in realistic hydrophilic confinement.An ab initio microscope: molecular contributions to the femtosecond time-dependent fluorescence shift of a Reichardt-type dye.Quantitative determination of site-specific conformational distributions in an unfolded protein by solid-state nuclear magnetic resonance.Dependence of protein folding stability and dynamics on the density and composition of macromolecular crowders.Non-bulk-like solvent behavior in the ribosome exit tunnel.Models of macromolecular crowding effects and the need for quantitative comparisons with experiment.Using simulations to provide the framework for experimental protein folding studiesProtein folding requires crowd control in a simulated cell.Macromolecular crowding induces polypeptide compaction and decreases folding cooperativityFree energy of nascent-chain folding in the translocon.Effect of interactions with the chaperonin cavity on protein folding and misfolding.Smoothing of the GB1 hairpin folding landscape by interfacial confinement.Biomolecular Crowding Arising from Small Molecules, Molecular Constraints, Surface Packing, and Nano-Confinement.Chemistry in nanoconfined water.Coil-globule transition of a single semiflexible chain in slitlike confinement.Protein folding in confined and crowded environments.Effect of the Solvent Temperatures on Dynamics of Serine Protease Proteinase KInteractions between amino acid side chains in cylindrical hydrophobic nanopores with applications to peptide stability.Thermodynamics and kinetics of protein folding under confinementConfinement effects on the kinetics and thermodynamics of protein dimerizationDevelopment of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin.Effects of interactions with the GroEL cavity on protein folding rates.Charge, hydrophobicity, and confined water: putting past simulations into a simple theoretical framework.Essential role of the chaperonin folding compartment in vivo.Enzyme entrapped in polymer-modified nanopores: the effects of macromolecular crowding and surface hydrophobicity.Combined effect of confinement and affinity of crowded environment on conformation switching of adenylate kinase.Helix formation inside a nanotube: possible influence of backbone-water hydrogen bonding by the confining surface through modulation of water activity.Effect of motional restriction on the unfolding properties of a cytochrome c featuring a His/Met-His/His ligation switch.Topology of polymer chains under nanoscale confinement.Nanopore Sensing of Protein Folding.Effect of the ordered water on protein folding: an off-lattice Gō-like model study.Environmental-confinement-induced stability enhancement of chiral molecules.Density of hydrophobically confined deeply cooled water investigated by small angle X-ray scattering.Phase Diagram of Water Confined by Graphene.Startling temperature effect on proteins when confined: single molecular level behaviour of human serum albumin in a reverse micelle.
P2860
Q24644640-99252D71-685C-4896-AEE0-537E8E17C13DQ26853115-B957AC28-53E6-4520-9BB6-39710E9A7783Q27315643-9038A7DD-E92B-4D3C-BBE8-835470287475Q28284812-E38A5EA2-5AF8-4C98-95D6-156172925F78Q28546403-5ED083A2-9846-4050-9F3B-CBCAB9AF4828Q30317092-39986CEF-42E2-454C-BDF0-2B49733025AEQ30317907-29942B95-0463-495D-BF5A-C4FC0ADD605BQ33489161-62FEA943-19F0-41F6-AF1F-BD497BB04FADQ33598985-398B7B2F-C1DD-471A-8CCB-E27BFE668D3DQ33727971-64E5A2FC-70A0-452B-B4A6-0986EC6E7562Q33788048-489B1BB8-81DB-4F8E-96BC-80C1B59EABCCQ33855688-641ADEA9-5385-46D3-B358-0DEF9B76F33DQ33938335-D7CAA1D0-4F1E-4781-9723-154548689D06Q34630145-3352302F-2926-4A1F-8C5C-B117D990BAA6Q34999575-AE4BC36F-6E3B-4F47-BFB9-3505543FA8FAQ36080242-41AEEFE2-8CCC-4F57-AC90-C6D1F66D3D50Q36150846-6636A99A-A9B4-46B4-BB22-063386C247E4Q36176612-B01342C5-D2B0-498F-A0E6-20FD893940C4Q36372696-3ABFBD1D-EF15-4166-8649-17965248CD56Q36382543-66D4067F-2A50-4B50-92EF-45D72D9421F1Q36420768-39A52095-BA4A-45C8-B254-F0C544551429Q36667206-3FD63C63-9383-47B3-935A-7DCD0B0EFD5BQ36976633-F2B3269C-FC76-4617-AEA8-55DD83FFA3D4Q37068635-E3E01EAF-0896-4D5E-925A-3ECC01A4CC90Q37153847-2AF69A10-1942-48D0-9236-660060E0F04CQ37245567-502D14D8-977E-4A7B-AAD9-4216F60DB803Q37409690-ED9865DA-A423-44DD-BA52-52C2DE19E350Q37670069-D754F2E9-3417-45B2-AD4A-A7645215748AQ38621639-2146DC26-8B15-4D07-8137-0BE6443AD44AQ44394914-59601E20-DA0A-4284-B840-8E6D4F3A9D62Q46809277-DC5D8163-9940-4E00-89EA-4186C8EE4874Q46829810-D4BC99DF-15A0-412C-A738-244B72EA62DFQ46933538-190FAB52-2A75-438F-A90A-20041061B90FQ47727177-54715F3F-2D16-41E7-87B1-626DF6B75D76Q47940837-25B9C89F-EAE8-47B0-B1FF-D0CB5361AD42Q47948316-8106E715-252E-4002-BE51-B864F3E0F27FQ50426604-09030A58-5599-4B67-B124-22254FF54740Q51729459-BE863C4A-E079-4C34-A1C0-CB489CBD5384Q52316604-C8D36705-6793-4397-B5D3-553AB7C01599Q53102194-AC8A28CA-F7B8-4B0D-BD4A-D55D60D5CEE7
P2860
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Protein folding under confinement: a role for solvent.
@ast
Protein folding under confinement: a role for solvent.
@en
type
label
Protein folding under confinement: a role for solvent.
@ast
Protein folding under confinement: a role for solvent.
@en
prefLabel
Protein folding under confinement: a role for solvent.
@ast
Protein folding under confinement: a role for solvent.
@en
P2093
P2860
P356
P1476
Protein folding under confinement: a role for solvent.
@en
P2093
Del Lucent
Vijay S Pande
P2860
P304
10430-10434
P356
10.1073/PNAS.0608256104
P407
P577
2007-06-11T00:00:00Z