Thermodynamics and kinetics of protein folding under confinement
about
Knotted proteins: A tangled tale of Structural BiologyConfinement and Stabilization of Fyn SH3 Folding Intermediate Mimetics within the Cavity of the Chaperonin GroEL Demonstrated by Relaxation-Based NMR.Small-angle neutron scattering studies of hemoglobin confined inside silica tubes of varying sizes.Dependence of protein folding stability and dynamics on the density and composition of macromolecular crowders.Knotting and unknotting proteins in the chaperonin cage: Effects of the excluded volumeModels of macromolecular crowding effects and the need for quantitative comparisons with experiment.Single-molecule spectroscopy of protein folding in a chaperonin cage.Free-energy landscape of the GB1 hairpin in all-atom explicit solvent simulations with different force fields: Similarities and differencesAssisted peptide folding by surface pattern recognition.Macromolecular crowding induces polypeptide compaction and decreases folding cooperativityPower-law dependence of the melting temperature of ubiquitin on the volume fraction of macromolecular crowders.Role of denatured-state properties in chaperonin action probed by single-molecule spectroscopyForce-induced unzipping transitions in an athermal crowded environment.Free 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.Modulation of folding kinetics of repeat proteins: interplay between intra- and interdomain interactions.Coil-globule transition of a single semiflexible chain in slitlike confinement.Using VIPT-jump to distinguish between different folding mechanisms: application to BBL and a Trpzip.Confinement effects on the kinetics and thermodynamics of protein dimerizationComputing protein stabilities from their chain lengths.Atomistic modeling of macromolecular crowding predicts modest increases in protein folding and binding stability.Model studies of the effects of intracellular crowding on nucleic acid interactions.Organization and dynamics of the N-terminal domain of chemokine receptor CXCR1 in reverse micelles: effect of graded hydration.Role of nonspecific interactions in molecular chaperones through model-based bioinformatics.Effects of crowding on the stability of a surface-tethered biopolymer: an experimental study of folding in a highly crowded regime.Conformational sampling of peptides in the presence of protein crowders from AA/CG-multiscale simulations.The ribosome modulates nascent protein folding.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.Nanoconfinement greatly speeds up the nucleation and the annealing in single-DNA collapse.Self-Collapsing of Single Molecular Poly-Propylene Oxide (PPO) in a 3D DNA Network.Steric confinement and enhanced local flexibility assist knotting in simple models of protein folding.The growth of filaments under macromolecular confinement using scaling theory.Entropy and enthalpy of interaction between amino acid side chains in nanopores.Amorphous Aggregation of Amyloid Beta 1-40 Peptide in Confined Space.The exclusive effects of chaperonin on the behavior of proteins with 52 knot.Denaturation and renaturation behaviors of short DNA in a confined space.Computational modeling highlights the role of the disordered Formin Homology 1 domain in profilin-actin transfer.
P2860
Q26783791-E7E84AD2-6EF9-499A-BFBB-85CD1E809069Q30008778-4A1F33DD-77EF-4E9C-A137-14285DEF58A4Q30356848-6C056A07-B523-4C68-A40B-B0C2D526AA85Q33598985-45E169D8-E0AC-4808-9901-2D467113DA40Q33657713-39512BF2-4769-42CD-B0A3-DADBC046B94AQ33788048-5D7E3F9F-F69D-49C5-A193-CD478BD13D99Q33977568-544095DE-E463-4916-AF5D-1F1D063A7AECQ34492990-385DD28F-C5F3-493F-8DD8-7247068D99B0Q34594687-AEE4B6A6-3A96-4658-9069-9F2387922F64Q34630145-FFDE7CE4-CAFD-4649-ADF7-17E52D59EEAFQ34722836-11C414A4-50EA-4C80-B78E-1489309C2ED0Q34727615-512FDC03-9D93-4652-B6BA-11620E7A15D5Q34780414-1E2722DA-8151-477C-AD54-EA4E0F1902C9Q34999575-A8A1B3CB-11B8-4B3D-A7D0-B3A370EE0587Q36080242-15787379-2EB5-4D8F-B073-E890AA3BF56FQ36150846-BCDFAF52-D202-4CC4-9A3B-9BB2820C1839Q36176612-5E64FB1E-F163-47A2-BD1F-C43DD2724927Q36317942-CC94A1CA-1824-4F66-B866-B42C557527CCQ36382543-DAF1921E-539A-42D0-B852-AC7B88C625AAQ36996200-0794953D-7474-45AC-BF3A-BA7CB8BD40B7Q37153847-DC1DC131-792F-4B97-8A88-65873A3DFD33Q37249879-20170F8F-79F1-4868-9C92-9596F780DC3FQ37263453-6FB8D0B1-64D8-4BB6-9C6F-7BBA330CFFD9Q39000630-B6B3A852-6500-4FCC-B0D8-745DDD03BE4DQ41867290-D06541CF-3436-48A2-9F47-36ADC24E2D9AQ41892008-EBDC29E7-1E97-49FC-9F9A-43DA0338A941Q41917327-18A734A6-8D54-463D-9EB6-15A91396C773Q41977797-AD0217E7-06F2-4054-ACBB-E9E0B8254B7CQ42714513-DEACD676-D042-417C-B8A5-6E133F8DDA2AQ44394914-2E2C538E-D592-48BE-B406-6D8E727E7F2DQ46809277-B75E664A-2276-4EDD-8B9F-42B7C685DBF0Q47861438-2651DB38-CF16-497E-B353-C62F252A1375Q48262012-4DFA9FC0-D707-41A0-8D0A-6ED8CB845F19Q48311966-19830A63-A4DF-4EC2-9040-A6A9B4E8552CQ51717614-C17DB4E6-46F0-4B74-AF5A-59D6215FAA85Q53245768-801CF6DC-A355-4339-9E0E-98D788E3DDFAQ53355595-BA42A713-0678-440E-9D92-83FCDAFF0AA3Q53432790-D5E3880E-B3E9-40DE-B205-1BD08495E6C9Q53483821-8E8B5325-72E6-4DF0-8C88-1F3F9E3ED71AQ55668102-29EF13B3-0DC1-49BA-9380-17769B2FE918
P2860
Thermodynamics and kinetics of protein folding under confinement
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 10 December 2008
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Thermodynamics and kinetics of protein folding under confinement
@en
Thermodynamics and kinetics of protein folding under confinement.
@nl
type
label
Thermodynamics and kinetics of protein folding under confinement
@en
Thermodynamics and kinetics of protein folding under confinement.
@nl
prefLabel
Thermodynamics and kinetics of protein folding under confinement
@en
Thermodynamics and kinetics of protein folding under confinement.
@nl
P2860
P356
P1476
Thermodynamics and kinetics of protein folding under confinement
@en
P2093
Jeetain Mittal
P2860
P304
20233-20238
P356
10.1073/PNAS.0807742105
P407
P577
2008-12-10T00:00:00Z