Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding (Q72033348)

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23 October 2019

title

Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding (English)

1 reference

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23 October 2019

3

Hartl FU

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23 October 2019

author name string

Hlodan R

series ordinal

1

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23 October 2019

Tempst P

series ordinal

2

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23 October 2019

publication date

1 July 1995

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Nature structural biology

23 October 2019

published in

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23 October 2019

volume

2

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23 October 2019

issue

7

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23 October 2019

page(s)

587-595

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Proteins as molecular chaperones.

23 October 2019

cites work

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

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ATP induces large quaternary rearrangements in a cage-like chaperonin structure.

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

31 March 2020

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A polypeptide bound by the chaperonin groEL is localized within a central cavity

31 March 2020

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Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

31 March 2020

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

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Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.

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The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.

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Refolding of barnase in the presence of GroE

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The chaperonin GroEL binds a polypeptide in an .alpha.-helical conformation

31 March 2020

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The covalent and tertiary structure of bovine liver rhodanese

31 March 2020

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A simple method for displaying the hydropathic character of a protein

31 March 2020

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Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP.

31 March 2020

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Different conformations for the same polypeptide bound to chaperones DnaK and GroEL.

31 March 2020

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Determination of the binding frame within a physiological ligand for the chaperone SecB.

31 March 2020

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The molten globule protein conformation probed by disulphide bonds

31 March 2020

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Protein folding. Solid evidence for molten globules

31 March 2020

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Residues in chaperonin GroEL required for polypeptide binding and release

31 March 2020

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GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

31 March 2020

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Unfolding and refolding of a type kappa immunoglobulin light chain and its variable and constant fragments

31 March 2020

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Kinetic characterization of early immunoreactive intermediates during the refolding of guanidine-unfolded Escherichia coli tryptophan synthase .beta.2 subunits

31 March 2020

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

31 March 2020

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Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

31 March 2020

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The helical hydrophobic moment: a measure of the amphiphilicity of a helix

31 March 2020

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Structure of myohemerythrin in the azidomet state at 1.7/1.3 A resolution

31 March 2020

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Side-chain torsional potentials: effect of dipeptide, protein, and solvent environment

31 March 2020

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31 March 2020

Identifiers

DOI

10.1038/NSB0795-587

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7664127%20AND%20SRC:MED&resulttype=core&format=json

23 October 2019

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