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The chaperonin GroEL binds to late-folding non-native conformations present in native Escherichia coli and murine dihydrofolate reductases

Journal of Molecular Biology

Jan 26, 1999

A C Clark, C Frieden

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Abstract

Dihydrofolate reductases from mouse (MuDHFR) or Escherichia coli (EcDHFR) are shown to refold via several intermediate forms, each of which can bind to the chaperonin GroEL. When stable complexes with GroEL are formed, they consist of late-folding intermediates. In addition, we find tha...read more

Mentioned in this Paper

Arsa
Thermodynamics
Tryptophan
GroEL Protein
HSPD1 gene
Dhfr
Alkalescens-Dispar Group
Nevus
Talpidae
Complex (molecular entity)
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The chaperonin GroEL binds to late-folding non-native conformations present in native Escherichia coli and murine dihydrofolate reductases

Journal of Molecular Biology

Jan 26, 1999

A C Clark, C Frieden

PMID: 9917411

DOI: 10.1006/jmbi.1998.2403

Abstract

Dihydrofolate reductases from mouse (MuDHFR) or Escherichia coli (EcDHFR) are shown to refold via several intermediate forms, each of which can bind to the chaperonin GroEL. When stable complexes with GroEL are formed, they consist of late-folding intermediates. In addition, we find tha...read more

Mentioned in this Paper

Arsa
Thermodynamics
Tryptophan
GroEL Protein
HSPD1 gene
Dhfr
Alkalescens-Dispar Group
Nevus
Talpidae
Complex (molecular entity)

Feeds With Similar Papers

Chaperones & Protein Folding

Chaperones are proteins that play an essential role in protein folding, stability, assembly, and degradation. Their depletion or dysfunction has been implicated in protein folding disorders. Here is the latest research.

Related Papers

Paper Details
References
  • References53
  • Citations12
12345...
  • References53
  • Citations12
12

Download from

Publisher
PubMed
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