Pages that link to "Q41632380"
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The following pages link to A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL. (Q41632380):
Displaying 33 items.
- ATP-bound states of GroEL captured by cryo-electron microscopy (Q27637162) (← links)
- Role of the -phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics (Q27642245) (← links)
- ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin (Q27678189) (← links)
- Chaperonin genes on the rise: new divergent classes and intense duplication in human and other vertebrate genomes (Q28748272) (← links)
- Out-of-equilibrium conformational cycling of GroEL under saturating ATP concentrations (Q33778946) (← links)
- Probing the functional mechanism of Escherichia coli GroEL using circular permutation (Q34058603) (← links)
- Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding (Q34545652) (← links)
- Probing the dynamic process of encapsulation in Escherichia coli GroEL. (Q35036090) (← links)
- Stimulating the substrate folding activity of a single ring GroEL variant by modulating the cochaperonin GroES. (Q35182853) (← links)
- Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle. (Q35676628) (← links)
- Spontaneous conformational changes in the E. coli GroEL subunit from all-atom molecular dynamics simulations (Q35963381) (← links)
- Engineering a nanopore with co-chaperonin function (Q36514091) (← links)
- Nucleotide-induced conformational changes of tetradecameric GroEL mapped by H/D exchange monitored by FT-ICR mass spectrometry (Q36605501) (← links)
- Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active state (Q36993737) (← links)
- Reconciling theories of chaperonin accelerated folding with experimental evidence (Q37620229) (← links)
- ATP-driven molecular chaperone machines (Q38123448) (← links)
- Harnessing proteasome dynamics and allostery in drug design. (Q38177328) (← links)
- Single-molecule observation of protein folding in symmetric GroEL-(GroES)2 complexes (Q42118511) (← links)
- High salt-induced conversion of Escherichia coli GroEL into a fully functional thermophilic chaperonin (Q43027849) (← links)
- Ionic interactions at both inter-ring contact sites of GroEL are involved in transmission of the allosteric signal: a time-resolved infrared difference study (Q43052174) (← links)
- Denatured proteins facilitate the formation of the football-shaped GroEL-(GroES)2 complex. (Q43178484) (← links)
- Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP. (Q43600500) (← links)
- Single-molecule observation of protein-protein interactions in the chaperonin system (Q43726756) (← links)
- Equilibrium and kinetics of the allosteric transition of GroEL studied by solution X-ray scattering and fluorescence spectroscopy (Q44340188) (← links)
- The allosteric transition of GroEL induced by metal fluoride-ADP complexes (Q44437566) (← links)
- Stopped-flow fluorescence analysis of the conformational changes in the GroEL apical domain: relationships between movements in the apical domain and the quaternary structure of GroEL. (Q44735766) (← links)
- GroEL mediates protein folding with a two successive timer mechanism. (Q44900588) (← links)
- Identification of a major inter-ring coupling step in the GroEL reaction cycle (Q44915287) (← links)
- Kinetic analysis of conformational changes of GroEL based on the fluorescence of tyrosine 506. (Q46219879) (← links)
- Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE. (Q54465588) (← links)
- GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle. (Q54536818) (← links)
- Refolding of target proteins from a "rigid" mutant chaperonin demonstrates a minimal mechanism of chaperonin binding and release (Q73850087) (← links)
- Chaperonin-assisted protein folding: a chronologue (Q89763905) (← links)