Protein folding: progress made and promises ahead - PubMed

Review

Protein folding: progress made and promises ahead

S E Radford. Trends Biochem Sci. 2000 Dec.

Abstract

Over the past 25 years, enormous breakthroughs have been made in understanding protein folding mechanisms. We have now reached an exciting stage, with consensuses beginning to emerge that combine both theoretical and experimental approaches. In addition, new fields have emerged and burgeoned, including in vivo folding and the study of protein misfolding diseases. In today's post-genomic world, understanding protein folding has never been more important and the topic has wide-ranging impact in fields from structural biology to materials science.

Similar articles

• Protein folding mechanisms: new methods and emerging ideas.

  Brockwell DJ, Smith DA, Radford SE. Brockwell DJ, et al. Curr Opin Struct Biol. 2000 Feb;10(1):16-25. doi: 10.1016/s0959-440x(99)00043-3. Curr Opin Struct Biol. 2000. PMID: 10679463 Review.

• Protein folding: a perspective for biology, medicine and biotechnology.

  Yon JM. Yon JM. Braz J Med Biol Res. 2001 Apr;34(4):419-35. doi: 10.1590/s0100-879x2001000400001. Braz J Med Biol Res. 2001. PMID: 11285453 Review.

• Exploring folding free energy landscapes using computational protein design.

  Kuhlman B, Baker D. Kuhlman B, et al. Curr Opin Struct Biol. 2004 Feb;14(1):89-95. doi: 10.1016/j.sbi.2004.01.002. Curr Opin Struct Biol. 2004. PMID: 15102454 Review.

• Recombinant protein folding and misfolding in Escherichia coli.

  Baneyx F, Mujacic M. Baneyx F, et al. Nat Biotechnol. 2004 Nov;22(11):1399-408. doi: 10.1038/nbt1029. Nat Biotechnol. 2004. PMID: 15529165 Review.

• Protein-based materials, toward a new level of structural control.

  van Hest JC, Tirrell DA. van Hest JC, et al. Chem Commun (Camb). 2001 Oct 7;(19):1897-904. doi: 10.1039/b105185g. Chem Commun (Camb). 2001. PMID: 12240211 Review.

Cited by

• Conformational Stability of the NH2-Terminal Propeptide of the Precursor of Pulmonary Surfactant Protein SP-B.

  Bañares-Hidalgo Á, Pérez-Gil J, Estrada P. Bañares-Hidalgo Á, et al. PLoS One. 2016 Jul 5;11(7):e0158430. doi: 10.1371/journal.pone.0158430. eCollection 2016. PLoS One. 2016. PMID: 27380171 Free PMC article.

• Refolding of a high molecular weight protein: salt effect on collapse.

  Lairez D, Pauthe E, Pelta J. Lairez D, et al. Biophys J. 2003 Jun;84(6):3904-16. doi: 10.1016/S0006-3495(03)75118-2. Biophys J. 2003. PMID: 12770896 Free PMC article.

• The Hsp70 chaperone system maintains high concentrations of active proteins and suppresses ATP consumption during heat shock.

  Hu B, Tomita M. Hu B, et al. Syst Synth Biol. 2007 Mar;1(1):47-58. doi: 10.1007/s11693-006-9004-2. Epub 2007 Jan 26. Syst Synth Biol. 2007. PMID: 19003436 Free PMC article.

• Equilibrium unfolding of A. niger RNase: pH dependence of chemical and thermal denaturation.

  Kumar GR, Sharma A, Kumari M, Jagannadham MV, Debnath M. Kumar GR, et al. Eur Biophys J. 2011 Aug;40(8):923-35. doi: 10.1007/s00249-011-0708-1. Epub 2011 May 25. Eur Biophys J. 2011. PMID: 21611854

• The Right-Handed Parallel β-Helix Topology of Erwinia chrysanthemi Pectin Methylesterase Is Intimately Associated with Both Sequential Folding and Resistance to High Pressure.

  Guillerm J, Frère JM, Meersman F, Matagne A. Guillerm J, et al. Biomolecules. 2021 Jul 22;11(8):1083. doi: 10.3390/biom11081083. Biomolecules. 2021. PMID: 34439750 Free PMC article.

Publication types

MeSH terms

LinkOut - more resources

• Full Text Sources

  • Elsevier Science

• Miscellaneous

  • NCI CPTAC Assay Portal