about
Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequencesInduced beta-barrel formation of the Alzheimer's Abeta25-35 oligomers on carbon nanotube surfaces: implication for amyloid fibril inhibitionEvaluating molecular mechanical potentials for helical peptides and proteinsConvergence of folding free energy landscapes via application of enhanced sampling methods in a distributed computing environment.Non-bulk-like solvent behavior in the ribosome exit tunnel.Models of macromolecular crowding effects and the need for quantitative comparisons with experiment.Macromolecular crowding induces polypeptide compaction and decreases folding cooperativityAdsorption mechanism and collapse propensities of the full-length, monomeric Aβ(1-42) on the surface of a single-walled carbon nanotube: a molecular dynamics simulation study.Protein folding under confinement: a role for solvent.Chemistry in nanoconfined water.Protein folding in confined and crowded environments.Interactions between amino acid side chains in cylindrical hydrophobic nanopores with applications to peptide stability.Thermodynamics and kinetics of protein folding under confinementFactors governing helix formation in peptides confined to carbon nanotubes.Charge, hydrophobicity, and confined water: putting past simulations into a simple theoretical framework.Under the lens: carbon nanotube and protein interaction at the nanoscale.Folding myoglobin within a sol-gel glass: protein folding constrained to a small volume.A bulk water-dependent desolvation energy model for analyzing the effects of secondary solutes on biological equilibria.An alpha-helical peptide in AOT micelles prefers to be localized at the water/headgroup interface.Probing hemoglobin confinement inside submicron silica tubes using synchrotron SAXS and electrochemical response.Energetics investigation on encapsulation of protein/peptide drugs in carbon nanotubes.Enantioselectivity of amino acids using chiral sensors based on nanotubes.Helix formation inside a nanotube: possible influence of backbone-water hydrogen bonding by the confining surface through modulation of water activity.Adsorption mechanism of an antimicrobial peptide on carbonaceous surfaces: A molecular dynamics study.Nanoconfinement in Slit Pores Enhances Water Self-Dissociation.Observations of the effect of confined space on fluorescence and diffusion properties of molecules in single conical nanopore channels.Peptide Folding in Translocon-Like Pores
P2860
Q24644640-E792D661-3602-4128-8C3B-F136F3A51AC7Q30157126-0584E360-D389-445C-A078-7DA35D9B522DQ33564099-C0382B2B-72EE-46B5-8CD8-E5848ACEC0B3Q33603629-81E69000-C0E8-4C40-B482-7E6E04B40D63Q33727971-119FC0BF-6B8B-4D54-B8B0-3DADB11561E4Q33788048-28DF4EB6-9A6E-4B0D-8D8A-E51E020E9190Q34630145-0460B005-77A7-4B65-9B9A-FCBB7DF768EBQ35895075-EA6D0FF8-D886-47ED-8C5B-BC08207DEA8EQ35973304-C7056930-CF7F-4B02-BF7E-E2B5FC94109AQ36372696-AD50064C-C499-45DE-8FBA-F6E61E93FE12Q36420768-9ED14D38-531A-4862-8150-F4DBE31CB3A7Q36976633-C75FA303-1D6D-491F-B14E-B9FF0A6B60F2Q37068635-2139534B-B646-4E9D-9697-F78CA31224ECQ37156632-2772AECC-D927-4499-9467-0C505DE5779CQ37670069-DC5CA111-B80F-40D0-A868-D3F1D5D66165Q38332800-38B85C6B-9588-4B31-9B5A-92BBE2612F27Q39122500-56ACA71D-6C86-4EC5-8942-CDBFD9D5A945Q39787640-8247AD04-902C-4CB2-99F3-6DF94CFA3493Q42538477-51A89E09-48DD-4769-B03D-DDC9648500CEQ43525759-1AD3A35C-F211-4FFE-A028-896AF51897F9Q45935566-6C344F26-F488-4CEE-99B3-F7C13DDE3AB4Q46076747-740F8230-6C29-4780-94E3-789AECCF6B3CQ46829810-0C366447-0BF4-4355-B4D5-467AC28F722EQ47962802-547F26F0-12B2-45C4-B218-F825E2913404Q49826038-5DC2F17F-B28E-4AFA-AE40-3756ADE77E67Q50541435-EDCA8D50-38B3-4700-9586-24B5AB427055Q58048706-7A92DBEE-8AEC-45F6-B4A7-E5CBA2E56477
P2860
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh
2006年學術文章
@zh-hant
name
Nanotube confinement denatures protein helices.
@en
Nanotube confinement denatures protein helices.
@nl
type
label
Nanotube confinement denatures protein helices.
@en
Nanotube confinement denatures protein helices.
@nl
prefLabel
Nanotube confinement denatures protein helices.
@en
Nanotube confinement denatures protein helices.
@nl
P356
P1476
Nanotube confinement denatures protein helices.
@en
P2093
Eric J Sorin
Vijay S Pande
P304
P356
10.1021/JA060917J
P407
P577
2006-05-01T00:00:00Z