Machinery of protein folding and unfolding

Curr Opin Struct Biol. 2002 Apr;12(2):231-8. doi: 10.1016/s0959-440x(02)00315-9.

Abstract

During the past two years, a large amount of biochemical, biophysical and low- to high-resolution structural data have provided mechanistic insights into the machinery of protein folding and unfolding. It has emerged that dual functionality in terms of folding and unfolding might exist for some systems. The majority of folding/unfolding machines adopt oligomeric ring structures in a cooperative fashion and utilise the conformational changes induced by ATP binding/hydrolysis for their specific functions.

Publication types

  • Review

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism
  • Chaperonin 10 / chemistry
  • Chaperonin 10 / metabolism
  • Chaperonin 60 / chemistry
  • Chaperonin 60 / metabolism
  • Chaperonin Containing TCP-1
  • Chaperonins / chemistry*
  • Chaperonins / metabolism*
  • Escherichia coli Proteins*
  • HSP70 Heat-Shock Proteins / chemistry
  • HSP70 Heat-Shock Proteins / metabolism
  • HSP90 Heat-Shock Proteins / chemistry
  • HSP90 Heat-Shock Proteins / metabolism
  • Hydrolysis
  • Models, Molecular
  • Molecular Chaperones / chemistry*
  • Molecular Chaperones / metabolism*
  • N-Ethylmaleimide-Sensitive Proteins
  • Protein Folding*
  • Vesicular Transport Proteins*

Substances

  • Carrier Proteins
  • Chaperonin 10
  • Chaperonin 60
  • Escherichia coli Proteins
  • HSP70 Heat-Shock Proteins
  • HSP90 Heat-Shock Proteins
  • Molecular Chaperones
  • Vesicular Transport Proteins
  • prefoldin
  • Adenosine Triphosphate
  • Chaperonin Containing TCP-1
  • Chaperonins
  • dnaK protein, E coli
  • N-Ethylmaleimide-Sensitive Proteins