Bacteriorhodopsin folds into the membrane against an external force.
about
Ultrastable atomic force microscopy: atomic-scale stability and registration in ambient conditionsImpact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins.One β hairpin follows the other: exploring refolding pathways and kinetics of the transmembrane β-barrel protein OmpG.Anisotropic deformation response of single protein molecules.Efficient unfolding pattern recognition in single molecule force spectroscopy data.Full reconstruction of a vectorial protein folding pathway by atomic force microscopy and molecular dynamics simulations.The applications of atomic force microscopy to vision science.Effect of particle diameter and surface composition on the spontaneous fusion of monolayer-protected gold nanoparticles with lipid bilayers.Improving single molecule force spectroscopy through automated real-time data collection and quantification of experimental conditions.Sequential unfolding of individual helices of bacterioopsin observed in molecular dynamics simulations of extraction from the purple membraneIn-Situ Observation of Membrane Protein Folding during Cell-Free ExpressionRoutine and timely sub-picoNewton force stability and precision for biological applications of atomic force microscopy.Membrane proteins scrambling through a folding landscape.Assembly and Stability of α-Helical Membrane Proteins.An unfolding story of helical transmembrane proteins.YidC assists the stepwise and stochastic folding of membrane proteinsFolding scene investigation: membrane proteins.Single molecule mechanical manipulation for studying biological properties of proteins, DNA, and sugars.Force-induced remodelling of proteins and their complexesHidden dynamics in the unfolding of individual bacteriorhodopsin proteins.Single-Molecule Force Spectroscopy Trajectories of a Single Protein and Its Polyproteins Are Equivalent: A Direct Experimental Validation Based on A Small Protein NuG2.Applications of Single-Molecule Methods to Membrane Protein Folding Studies.Direct observation of active protein folding using lock-in force spectroscopy.The viscoelasticity of membrane tethers and its importance for cell adhesion.Electrostatic and steric interactions determine bacteriorhodopsin single-molecule biomechanics.The effect of different force applications on the protein-protein complex Barnase-Barstar.Velocity-dependent mechanical unfolding of bacteriorhodopsin is governed by a dynamic interaction networkFree energy of membrane protein unfolding derived from single-molecule force measurements.Single molecule compression reveals intra-protein forces drive cytotoxin pore formation.Toward a molecular understanding of the anisotropic response of proteins to external forces: insights from elastic network models.Forced Unfolding Mechanism of Bacteriorhodopsin as Revealed by Coarse-Grained Molecular Dynamics.Multiparametric high-resolution imaging of native proteins by force-distance curve-based AFM.Improved free-energy landscape reconstruction of bacteriorhodopsin highlights local variations in unfolding energy.Atomic force microscopy-based characterization and design of biointerfaces
P2860
Q24632615-6CAD163D-BAE2-452C-BCFE-9842EDC80BA0Q30152825-1052DAFE-BEE3-4EDC-8689-A9CCCE3BBF56Q30155528-DA036D6A-C76D-45A1-8E73-C306B9745FE9Q30356256-8F14DE65-B5E4-45E1-A803-3593770D19F6Q30403477-55BC98B1-C913-4F83-A42E-37E2A948BC2AQ30497468-26F81B85-2FD6-4CF0-B4AA-B40A64D2E70BQ33760294-5FA79684-884F-4DBC-B7D0-C3E14EA2B564Q34253700-AA8DE4EF-488C-453D-AD5F-382CFAF8D45DQ34977712-6DCF2866-C74C-48C5-B259-E882E59F8231Q35095833-38771412-E748-424B-9A54-859EF5A61E61Q35957752-8FEC07D9-91C8-4106-98DF-1F7457A7B626Q36095671-D64CA872-0B82-4447-85D3-AA5270277526Q36296039-66C66848-2596-4148-BBA7-36D1D0330FE0Q36405729-93619B4D-1726-4AAF-B6F1-B3CD6447B599Q36673002-E628CD67-61B3-4A8F-9BFA-C9404FE6841FQ37348184-DB2C59BA-DA00-45E7-A6C4-D181023DB4F1Q37373862-1CD9DABB-246E-4EB3-8CA1-704BC96BF8D5Q38172064-66253F16-7E66-447C-8CA8-55C203DB82FDQ38364742-1B7BE891-4402-4AA7-A672-6C0DBA55A337Q38932283-499ACBE2-1B35-471F-A8B9-09517BFFBFE3Q39062760-EE5F3446-37CB-4258-BEE4-67E04C46278EQ39333393-C5151D5C-6D9F-40B2-9636-6A93A98AAEF7Q40321082-BB557233-0093-43EC-ACEC-634175EA35B1Q40768635-79D08D97-95E6-4991-8C9F-570F60B8831BQ42183576-F6018C5B-C8A9-4178-AD79-0388A0A32789Q42551778-FEC4C3B6-AA19-4F86-8CE6-CBFD57A0B358Q42595740-2D1E703F-03C7-4D05-B4E2-9C1CC85758DBQ42626754-E7258197-8F65-4E6A-BD37-15A8B77FB4F2Q42684620-0348504D-D283-4EEE-A66F-FB90DAFB7023Q43111576-68F92561-DAB0-4389-A478-E14CAC5D49DDQ46152840-6E43A0B8-BBF4-430F-92BC-B3DAED033132Q48315684-4DE5DF93-4F30-4C79-8D22-A7F909EA3F70Q52616500-4A638F58-3838-428A-8B90-D55AFE418437Q57825230-91EF5A10-CED0-4EE1-9F79-93982F12DABD
P2860
Bacteriorhodopsin folds into the membrane against an external force.
description
2006 nî lūn-bûn
@nan
2006 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Bacteriorhodopsin folds into the membrane against an external force.
@ast
Bacteriorhodopsin folds into the membrane against an external force.
@en
type
label
Bacteriorhodopsin folds into the membrane against an external force.
@ast
Bacteriorhodopsin folds into the membrane against an external force.
@en
prefLabel
Bacteriorhodopsin folds into the membrane against an external force.
@ast
Bacteriorhodopsin folds into the membrane against an external force.
@en
P2093
P1476
Bacteriorhodopsin folds into the membrane against an external force.
@en
P2093
Harald Janovjak
Hermann E Gaub
Kay E Gottschalk
Max Kessler
P304
P356
10.1016/J.JMB.2005.12.065
P407
P577
2006-01-06T00:00:00Z