Global minimization of an off-lattice potential energy function using a chaperone-based refolding method (Q74615738)

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12 November 2019

title

Global minimization of an off-lattice potential energy function using a chaperone-based refolding method (English)

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12 November 2019

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Gorse D

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12 November 2019

publication date

1 November 2001

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12 November 2019

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12 November 2019

volume

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12 November 2019

issue

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12 November 2019

page(s)

411-426

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In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System

12 November 2019

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding

21 January 2018

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A structural model for GroEL-polypeptide recognition

21 January 2018

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Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism

21 January 2018

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Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

21 January 2018

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Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage

21 January 2018

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GroEL-GroES-mediated protein folding requires an intact central cavity

21 January 2018

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The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding

21 January 2018

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The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

21 January 2018

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21 January 2018

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Protein folding Folding with a two-stroke motor

21 January 2018

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Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

21 January 2018

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Statistical mechanics of kinetic proofreading in protein folding in vivo

21 January 2018

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Simulations of chaperone-assisted folding.

21 January 2018

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GroE facilitates refolding of citrate synthase by suppressing aggregation

21 January 2018

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Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

21 January 2018

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Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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Secondary structure forming propensity coupled with amphiphilicity is an optimal motif in a peptide or protein for association with chaperonin 60 (GroEL)

21 January 2018

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The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity

21 January 2018

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Linking topography of its potential surface with the dynamics of folding of a protein model

21 January 2018

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Folding funnels and frustration in off-lattice minimalist protein landscapes

21 January 2018

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Nature and consequences of GroEL-protein interactions.

21 January 2018

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Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL 1 1Edited by J. Karn

21 January 2018

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Calorimetric Observation of a GroEL-Protein Binding Reaction with Little Contribution of Hydrophobic Interaction

21 January 2018

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21 January 2018

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Minimum energy compact structures of random sequences of heteropolymers

21 January 2018

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Role of potential-energy scaling in the low-temperature relaxation behavior of amorphous materials

21 January 2018

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A strategy for finding classes of minima on a hypersurface: implications for approaches to the protein folding problem

21 January 2018

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An approach to the multiple-minima problem in protein folding by relaxing dimensionality. Tests on enkephalin.

21 January 2018

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GroEL-substrate interactions: molding the fold, or folding the mold?

21 January 2018

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RASMOL: biomolecular graphics for all

21 January 2018

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COCI

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10.1002/1097-0282(200111)59:6<411::AID-BIP1046>3.0.CO;2-J

12 August 2024

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