Overview of Protein Folding

Roger H. Pain1

1 Jozef Stefan Institute, Ljubljana
Publication Name:  Current Protocols in Protein Science
Unit Number:  Unit 6.4
DOI:  10.1002/0471140864.ps0604s00
Online Posting Date:  May, 2001
GO TO THE FULL TEXT: PDF or HTML at Wiley Online Library

Abstract

This overview discusses aspects of protein folding including aggregation, folding pathways, disulfide bonds, stabilization of the native functional state, and approaches for achieving an acceptable rate of protein folding starting with a denatured polypeptide.

     
 
GO TO THE FULL PROTOCOL:
PDF or HTML at Wiley Online Library

Table of Contents

  • How Proteins Fold
  • How to Fold Proteins
  • Literature Cited
  • Figures
     
 
GO TO THE FULL PROTOCOL:
PDF or HTML at Wiley Online Library

Materials

GO TO THE FULL PROTOCOL:
PDF or HTML at Wiley Online Library

Figures

Videos

Literature Cited

Literature Cited
   Anfinsen, C.B. 1967. The formation of the tertiary structure of proteins. Harvey Lect. 61:95‐116.
   Anfinsen, C.B. 1973. Principles that govern the folding of protein chains. Science 181:223‐230.
   Craig, S., Schmeissner, U., Wingfield, P., and Pain, R.H. 1987. Conformation, stability and folding of interleukin‐1β. Biochemistry 26:3570‐3576.
   Gilbert, H.F. 1994. The formation of native disulfide bonds. In Mechanisms of Protein Folding (R.H. Pain, ed.) pp. 109‐111. Oxford University Press, Oxford.
   Goloubinoff, P., Christeller, J.T., Gatenby, A.A., and Lorimer, G.H. 1989. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperone proteins and ATP. Nature 342:884‐889.
   Haase‐Pettingell, C.A. and King, J. 1988. Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tail spike maturation. J. Biol. Chem. 263:4977‐4983.
   Hlodan, R., Craig, S., and Pain, R.H. 1991. Protein folding and its implications for the production of recombinant proteins. Biotechnol. & Genet. Eng. Rev. 9:47‐88.
   Hlodan, R. and Hartl, F.U. 1994. How the protein folds in the cell. In Mechanisms of Protein Folding (R.H. Pain, ed.) pp. 194‐228. Oxford University Press, Oxford.
   Lapanje, S., Skerjane, J., Glavnik, S., and Zibret, S. 1978. Thermodynamic studies of the interactions of guanidinium chloride and urea with some oligoglycines and oligolysines. J. Chem. Thermodynam. 10:425‐433.
   Lindsay, C.D. and Pain, R.H. 1991. Refolding and assembly of penicillin acylase, an enzyme composed of two polypeptide chains that result from proteolytic activation. Biochemistry 30:9034‐9040.
   Lomas, D.A., Evans, D.Ll., Stone, S.R., Chang, W.‐S.W., and Carrell, R.W. 1993. Effect of the Z mutation on the physical and inhibitory properties of α1‐antitrypsin. Biochemistry 32:500‐508.
   Mitchinson, C. and Pain, R.H. 1985. Effects of sulfate and urea on the stability and reversible unfolding of β‐lactamase from Staphylococcus aureus. J. Mol. Biol. 184:331‐342.
   Nall, B.T. 1994. Proline isomerization as a rate‐limiting step. In Mechanisms of Protein Folding (R.H. Pain, ed.) pp. 80‐103. Oxford University Press, Oxford.
   Ptitsyn, O.B., Pain, R.H., Semisotnov, G.V., Zerovnik, E., and Razgulaev, D.I. 1990. Evidence for a molten globule state as a general intermediate in protein folding. FEBS (Fed. Eur. Biochem. Soc.) Lett. 262:20‐24.
   Roder, H. and Elöve, G.A. 1994. Early stages of protein folding. In Mechanisms of Protein Folding (R.H. Pain, ed.) pp. 37‐40. Oxford University Press, Oxford.
   Thatcher, D. and Hitchcock, A. 1994. Protein folding in biotechnology. In Mechanisms of Protein Folding (R.H. Pain, ed.) pp. 242‐250. Oxford University Press, Oxford.
GO TO THE FULL PROTOCOL:
PDF or HTML at Wiley Online Library