Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering. (Q53992724)

23 May 2018

title

Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering. (English)

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23 May 2018

author name string

Thiyagarajan P

series ordinal

1

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23 May 2018

Henderson SJ

series ordinal

2

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23 May 2018

Joachimiak A

series ordinal

3

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23 May 2018

publication date

1 January 1996

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23 May 2018

published in

Structure

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23 May 2018

volume

4

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23 May 2018

issue

1

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23 May 2018

page(s)

79-88

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23 May 2018

Young Investigator Award Lecture. Structures of larger proteins, protein-ligand and protein-DNA complexes by multidimensional heteronuclear NMR.

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Molecular chaperone functions of heat-shock proteins

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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Symmetric complexes of GroE chaperonins as part of the functional cycle

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

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

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Residues in chaperonin GroEL required for polypeptide binding and release

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

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Mutation Ala2-->Ser destabilizes intersubunit interactions in the molecular chaperone GroEL.

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The strongly conserved carboxyl-terminus glycine-methionine motif of the Escherichia coli GroEL chaperonin is dispensable.

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A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K-12.

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Two-dimensional crystals of the molecular chaperone GroEL reveal structural plasticity.

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The molecular chaperonin cpn60 displays local flexibility that is reduced after binding with an unfolded protein

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Conformational cycle of the archaeosome, a TCP1-like chaperonin from Sulfolobus shibatae

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Solution X-ray scattering study on the chaperonin GroEL from Escherichia coli.

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A mutant at position 87 of the GroEL chaperonin is affected in protein binding and ATP hydrolysis.

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

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Folding intermediate binds to the bottom of bullet-shaped holo-chaperonin and is readily accessible to antibody.

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Absolute calibration of small-angle neutron scattering data

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10.1016/S0969-2126(96)00011-1

Identifiers

DOI

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23 May 2018

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23 May 2018