ArticleProceedings of the National Academy of Sciences of the United States of America2005
Direct NMR observation of a substrate protein bound to the chaperonin GroEL.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- From Microstates to Macrostates in the Conformational Dynamics of GroEL: A Single-Molecule Förster Resonance Energy Transfer Study.The journal of physical chemistry letters · 2023Article
- Dissecting the Thermodynamics of ATP Binding to GroEL One Nucleotide at a Time.ACS central science · 2023Article
- GroEL-A Versatile Chaperone for Engineering and a Plethora of Applications.Biomolecules · 2022Review
- Evolutionarily Related Dihydrofolate Reductases Perform Coequal Functions Yet Show Divergence in Their Trajectories.The protein journal · 2018Review
- Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins.Nature chemical biology · 2018Article
- Article
- Chloroplast Chaperonin: An Intricate Protein Folding Machine for Photosynthesis.Frontiers in molecular biosciences · 2017Review
- Decoding Structural Properties of a Partially Unfolded Protein Substrate: En Route to Chaperone Binding.PLoS computational biology · 2015Article
- Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?Archives of biochemistry and biophysics · 2014Review
- Structural basis for protein antiaggregation activity of the trigger factor chaperone.Science (New York, N.Y.) · 2014Article
- GroEL/ES chaperonin modulates the mechanism and accelerates the rate of TIM-barrel domain folding.Cell · 2014Article
- Seeing the invisible by paramagnetic and diamagnetic NMR.Biochemical Society transactions · 2013Article
- ATP-driven molecular chaperone machines.Biopolymers · 2013Review
- Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp.Nature structural & molecular biology · 2013Article
- Chaperonin-mediated protein folding.The Journal of biological chemistry · 2013Article
- Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Identification of endogenous ligands bound to bacterially expressed human and E. coli dihydrofolate reductase by 2D NMR.FEBS letters · 2011Article
- Nuclear magnetic resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL.Protein science : a publication of the Protein Society · 2011Article
- Simulation of chaperonin effect on protein folding: a shift from nucleation-condensation to framework mechanism.Journal of the American Chemical Society · 2011Article
- Protein folding in the cytoplasm and the heat shock response.Cold Spring Harbor perspectives in biology · 2010Review
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6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The reaction cycle and the major structural states of the molecular chaperone GroEL and its cochaperone, GroES, are well characterized. In contrast, very little is known about the nonnative states of the substrate polypeptide acted on by the chaperonin machinery. In this study, we investigated the substrate protein human dihydrofolate reductase (hDHFR) while bound to GroEL or to a single-ring analog, SR1, by NMR spectroscopy in solution under conditions where hDHFR was efficiently recovered as a folded, enzymatically active protein from the stable complexes upon addition of ATP and GroES. By using the NMR techniques of transverse relaxation-optimized spectroscopy (TROSY), cross-correlated relaxation-induced polarization transfer (CRIPT), and cross-correlated relaxation-enhanced polarization transfer (CRINEPT), bound hDHFR could be observed directly. Measurements of the buildup of hDHFR NMR signals by different magnetization transfer mechanisms were used to characterize the dynamic properties of the NMR-observable parts of the bound substrate. The NMR data suggest that the bound state includes random coil conformations devoid of stable native-like tertiary contacts and that the bound hDHFR might best be described as a dynamic ensemble of randomly structured conformers.
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