Photoincorporation of fluorescent probe into GroEL: defining site of interaction (Q30430105)

21 June 2017

title

Photoincorporation of fluorescent probe into GroEL: defining site of interaction (English)

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21 June 2017

Seale JW

1

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21 June 2017

Brazil BT

series ordinal

2

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21 June 2017

Horowitz PM

series ordinal

3

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21 June 2017

language of work or name

English

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publication date

1 January 1998

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21 June 2017

published in

Methods in Enzymology

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21 June 2017

volume

290

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21 June 2017

page(s)

318-323

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Model peptide studies demonstrate that amphipathic secondary structures can be recognized by the chaperonin GroEL (cpn60)

21 June 2017

cites work

1 reference

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7 January 2021

The hydrophobic nature of GroEL-substrate binding

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7 January 2021

Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. I. GroEL recognizes the signal sequences of beta-lactamase precursor.

1 reference

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7 January 2021

Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature beta-lactamase.

1 reference

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7 January 2021

Evidence for a molten globule state as a general intermediate in protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990028-3

7 January 2021

High hydrostatic pressure induces the dissociation of cpn60 tetradecamers and reveals a plasticity of the monomers.

1 reference

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7 January 2021

Topology of the Na,K-ATPase. Evidence for externalization of a labile transmembrane structure during heating

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7 January 2021

Dimer formation from 1-amino-8-naphthalenesulfonate catalyzed by bovine serum albumin. A new fluorescent molecule with exceptional binding properties

1 reference

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7 January 2021

Protein conformational changes induced by 1,1'-bis(4-anilino-5-naphthalenesulfonic acid): preferential binding to the molten globule of DnaK.

1 reference

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7 January 2021

Photoincorporation of 4,4'-bis(1-anilino-8-naphthalenesulfonic acid) into the apical domain of GroEL: specific information from a nonspecific probe

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990028-3

7 January 2021

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990028-3

7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990028-3

7 January 2021

The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.

1 reference

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7 January 2021

10.1016/S0076-6879(98)90028-3

Identifiers

DOI

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21 June 2017

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