Single-molecule spectroscopy of protein folding in a chaperonin cage. - Wikidata - awgldk - TriplyDB

Single-molecule spectroscopy of protein folding in a chaperonin cage.

Single-molecule spectroscopy of protein folding in a chaperonin cage.

http://www.wikidata.org/entity/Q33977568

about

The dynamic conformational cycle of the group I chaperonin C-termini revealed via molecular dynamics simulation Structural heterogeneity and quantitative FRET efficiency distributions of polyprolines through a hybrid atomistic simulation and Monte Carlo approach GroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain Folding Protein folding at single-molecule resolution.Native and unfolded states of phosphoglycerate kinase studied by single-molecule FRET.Micro total analysis systems for cell biology and biochemical assays Probing water density and dynamics in the chaperonin GroEL cavity.Quantifying heterogeneity and conformational dynamics from single molecule FRET of diffusing molecules: recurrence analysis of single particles (RASP).Fast single-molecule FRET spectroscopy: theory and experiment Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein.FRET efficiency distributions of multistate single molecules.Mechanisms of cellular proteostasis: insights from single-molecule approaches Role of denatured-state properties in chaperonin action probed by single-molecule spectroscopy Visualizing a one-way protein encounter complex by ultrafast single-molecule mixing.Protein folding in the cell: challenges and progress.Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins Determining serpin conformational distributions with single molecule fluorescence Effect of interactions with the chaperonin cavity on protein folding and misfolding.Förster resonance energy transfer: Role of diffusion of fluorophore orientation and separation in observed shifts of FRET efficiency.Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy.Localizing internal friction along the reaction coordinate of protein folding by combining ensemble and single-molecule fluorescence spectroscopy Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding.Effects of interactions with the GroEL cavity on protein folding rates.Shedding light on protein folding landscapes by single-molecule fluorescence.Fluorescence anisotropy and resonance energy transfer: powerful tools for measuring real time protein dynamics in a physiological environment.Recent advances in single-molecule detection on micro- and nano-fluidic devices.Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions.How do chaperonins fold protein?The chaperone toolbox at the single-molecule level: From clamping to confining.Chaperone-client interactions: Non-specificity engenders multifunctionality.Folding while bound to chaperones.Unconventional Kondo effect in redox active single organic macrocyclic transistors.Role of nonspecific interactions in molecular chaperones through model-based bioinformatics.Double mutant MBP refolds at same rate in free solution as inside the GroEL/GroES chaperonin chamber when aggregation in free solution is prevented Single-molecule measurements of transient biomolecular complexes through microfluidic dilution.A sticky cage can slow down folding.Microfluidic mixer designed for performing single-molecule kinetics with confocal detection on timescales from milliseconds to minutes.Single Pair Förster Resonance Energy Transfer: A Versatile Tool To Investigate Protein Conformational Dynamics.Folding of maltose binding protein outside of and in GroEL.Slow Interconversion in a Heterogeneous Unfolded-State Ensemble of Outer-Membrane Phospholipase A.

P2860

Q27315643-0804550C-203B-4E3D-8068-42E18EF57C8E Q27342193-A319755F-2C6F-4B21-8699-626527298340 Q27683698-ACF7DE23-9565-495C-8F10-E02A09232F5A Q30399457-B031C1DD-73A7-43EB-8B96-DEEAE2209FB6 Q30400065-5B62CE18-2A20-4C2B-9A5A-BF486A573535 Q30459045-024006D3-8ACD-4D73-BDF6-B32FB5A0965D Q30828360-6DB68D15-5CE0-47DF-AFA3-11B4DB8C70E9 Q33789209-2AA8759C-4189-460A-ADC1-5595E51D9DAE Q34135228-4037BBE3-CBCC-43F8-8F94-A214AEF13147 Q34218169-056DCDDF-F63E-4A2F-87F1-D16354516666 Q34336575-D38E4397-8061-4D21-A8F3-8591376102B9 Q34422820-47ED68DA-C43C-4DEF-8A53-020125B64E0B Q34727615-5DAD3880-758E-474C-8F4C-AC5885AACB1D Q34767840-9A4274B7-1F5E-47FD-AA2E-951939BCEDA4 Q34768822-06D8CFCE-B6F3-4BE2-9E03-EC211A6FF847 Q35177787-629E9659-2DE1-4A6C-A8FC-2E4B63F51796 Q36058093-29AB0B25-D260-43F3-A38C-8B479F81E257 Q36080242-98402F1C-5A58-49D4-9651-EACC0BD9F796 Q36380127-A303535D-1CCC-43FB-9A26-B738F7DD94E5 Q36398007-E32EB9A0-199D-440D-ABE9-1C36A3BBEBD1 Q36445621-4C949783-3533-45C1-B0AD-DCBA1179E345 Q37312135-1C00110D-7A63-470E-B911-D1697ACF0D58 Q37409690-DB9D3824-D9C5-41A8-906C-15D50954FA4E Q37645549-F9C7ECB6-5C03-4CD3-836A-67672EF7F9C9 Q37802709-CFA7F999-1029-4BE0-A78A-7625B8CCE614 Q37963804-11F589CE-956D-4EF3-A80A-2F0B80B72F1E Q38095686-18053690-7CF7-463F-BA42-42EF7A33DF5C Q38919368-41F4F10A-863C-410D-94CF-D03C86EF1FC7 Q39200186-AE043C86-E40B-4F51-9C43-DFB1421D0146 Q39376939-13A94C8E-962E-41D7-B454-1B212D3E372F Q39451710-4D067BC4-0C2E-4BF9-928F-DE454CD3B4A3 Q39499308-D2C09EAB-F874-47E7-871B-D25F603A9437 Q41892008-9BAC605B-1EBD-442D-9473-DD668AB1915D Q42255381-8A2F6559-5590-49D0-A8BD-C604AEE567BD Q42561896-D7B07802-799D-4BCB-9A99-6902072E5BF9 Q42779750-E69F5896-E8B6-47ED-B0EF-4C5F8D2B41E8 Q44589111-48F84A72-DDAA-45E2-BE35-BE534317BB91 Q47219286-09BB1409-464F-4B6A-B307-5D1B503451A6 Q47236838-D2884539-F57F-48D5-8D60-74DAE77DC8DD Q50577647-1F072D18-D8DF-4B2D-AFCA-032ADB0BDB0B

P2860

Single-molecule spectroscopy of protein folding in a chaperonin cage.

http://www.wikidata.org/entity/Q33977568

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Single-molecule spectroscopy of protein folding in a chaperonin cage.

@ast

Single-molecule spectroscopy of protein folding in a chaperonin cage.

@en

type

label

Single-molecule spectroscopy of protein folding in a chaperonin cage.

@ast

Single-molecule spectroscopy of protein folding in a chaperonin cage.

@en

prefLabel

Single-molecule spectroscopy of protein folding in a chaperonin cage.

@ast

Single-molecule spectroscopy of protein folding in a chaperonin cage.

@en

P1433

Q33977568-32F59495-CF46-48B5-AFCD-B31FD9E3D8A0

P1476

Q33977568-56548485-A7C5-4454-82C9-E2E8670E0DB5

P2093

Q33977568-079815C7-6747-4942-8883-35F09A8E1974

Q33977568-2F6D9C55-1A1C-4FA8-B6DE-1E348A652CB4

Q33977568-326729C3-9639-4D48-A670-F1EE21CB5871

Q33977568-5D2081A9-5363-40DA-A4AC-222783F15AF8

Q33977568-6D26002E-E296-41A1-A505-169FE1A7A058

Q33977568-76DB2383-9321-4429-8760-3B56AB7EBA7A

Q33977568-A9FD76B9-640A-41A2-82CA-780FE796E238

Q33977568-D7480A9F-E4F1-4A7B-B2FE-631315F32C54

P2860

Q33977568-0473D26A-428E-40C7-8CA8-369F7DD91CDE

Q33977568-0497F442-3C65-455A-B97A-3B75F42087C0

Q33977568-0CD61FCB-C367-4F14-A055-C6AF8F3DDB81

Q33977568-0CEE538C-785F-484A-9DB5-CA05B70B12A7

Q33977568-0EEEEA81-9445-42C1-8B83-459EABF707BF

Q33977568-16FDAFC0-2ECB-423D-9212-C3F8FD1E3CBD

Q33977568-20DCF6DD-D0CB-46A5-A9FE-F49A417AD2FE

Q33977568-24563B38-20B2-4497-9B07-ED0DE6C6E605

Q33977568-25590AFE-802E-4D2A-9234-F0ECCE930F3E

Q33977568-27C1C75E-2986-4CB3-B5EA-4588FF816FFF

P304

Q33977568-58C916BA-41EB-4D25-A7EF-F2CB6416BD78

P31

Q33977568-6B10D91D-5F49-4CB5-A758-9DA945A945B3

P356

Q33977568-88AA902F-E5CB-4886-9590-8FD0F2046A01

P407

Q33977568-33FD3479-065D-4220-9C35-A0B9136F5AFD

P433

Q33977568-BC3E9A6F-9D85-49BC-AED7-F33C35FAE056

P478

Q33977568-84ED242E-C144-4A8B-8F0A-714C3C50AF37

P50

Q33977568-D8C4C030-000D-438C-92AA-CB01D77DBB1D

P577

Q33977568-04592A33-4677-475D-9C24-B41D795651FA

P5875

Q33977568-EA5F0C81-C0A9-4FB3-AEE2-42DE7F700B44

P698

Q33977568-E1D2BB71-376A-4766-85EF-10DE5E9496F6

P921

Q33977568-DA62C7C8-4B15-4637-98B0-34DA3DBD014E

P932

Q33977568-2A603BE3-F746-4A72-AA81-B8EA2DA86CF6

P356

PNAS.1002356107

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Single-molecule spectroscopy of protein folding in a chaperonin cage

@en

P2093

Armin Hoffmann

http://www.w3.org/2001/XMLSchema#string

Daniel Nettels

http://www.w3.org/2001/XMLSchema#string

Daniel Streich

http://www.w3.org/2001/XMLSchema#string

Dominik Haenni

http://www.w3.org/2001/XMLSchema#string

Everett A Lipman

http://www.w3.org/2001/XMLSchema#string

Frank Hillger

http://www.w3.org/2001/XMLSchema#string

Hagen Hofmann

http://www.w3.org/2001/XMLSchema#string

Shawn H Pfeil

http://www.w3.org/2001/XMLSchema#string

P2860

Chaperonin chamber accelerates protein folding through passive action of preventing aggregation

The effect of macromolecular crowding on chaperonin-mediated protein folding

Role of the -phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics

Molecular chaperones in the cytosol: from nascent chain to folded protein

Funnels, pathways, and the energy landscape of protein folding: a synthesis

Molecular chaperones and protein quality control

Quality control in the endoplasmic reticulum

Fast kinetics and mechanisms in protein folding.

Fluorescence-aided molecule sorting: analysis of structure and interactions by alternating-laser excitation of single molecules.

Measuring internal friction of an ultrafast-folding protein

P304

11793-11798

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.1002356107

http://www.w3.org/2001/XMLSchema#string

P407

P433

26

http://www.w3.org/2001/XMLSchema#string

P478

107

http://www.w3.org/2001/XMLSchema#string

P50

Benjamin Schuler

P577

2010-06-14T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

44673052

http://www.w3.org/2001/XMLSchema#string

P698

20547872

http://www.w3.org/2001/XMLSchema#string

P921

protein folding

P932

2900638

http://www.w3.org/2001/XMLSchema#string