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Literature DB >> 8011615

Kinetics versus thermodynamics in protein folding.

Abstract

Until quite recently it has been generally believed that the observed tertiary structure of a protein is controlled by thermodynamic and not kinetic processes. In this essay we review several recent results which call into question the universality of the thermodynamic hypothesis and discuss their implications for the understanding of protein folding.

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Year: 1994 PMID： 8011615 DOI： 10.1021/bi00190a002

Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162

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Cited

55 in total

Review 1. Folding funnels, binding funnels, and protein function.

Authors: C J Tsai; S Kumar; B Ma; R Nussinov
Journal: Protein Sci Date: 1999-06 Impact factor: 6.725

2. Distinguishing between sequential and nonsequentially folded proteins: implications for folding and misfolding.

Authors: C J Tsai; J V Maizel; R Nussinov
Journal: Protein Sci Date: 1999-08 Impact factor: 6.725

Review 3. Folding and binding cascades: dynamic landscapes and population shifts.

Authors: S Kumar; B Ma; C J Tsai; N Sinha; R Nussinov
Journal: Protein Sci Date: 2000-01 Impact factor: 6.725

4. Alpha-to-beta structural transformation of ovalbumin: heat and pH effects.

Authors: H Y Hu; H N Du
Journal: J Protein Chem Date: 2000-04

Review 5. Protein folding.

Authors: M A Basharov
Journal: J Cell Mol Med Date: 2003 Jul-Sep Impact factor: 5.310

10. In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: implications for protein folding and assembly.

Authors: P Zhang; H K Schachman
Journal: Protein Sci Date: 1996-07 Impact factor: 6.725

Kinetics versus thermodynamics in protein folding.

Review 1. Folding funnels, binding funnels, and protein function.

2. Distinguishing between sequential and nonsequentially folded proteins: implications for folding and misfolding.

Review 3. Folding and binding cascades: dynamic landscapes and population shifts.

4. Alpha-to-beta structural transformation of ovalbumin: heat and pH effects.

Review 5. Protein folding.

Review 6. How do proteins avoid becoming too stable? Biophysical studies into metastable proteins.

7. Probing protein stability and proteolytic resistance by loop scanning: a comprehensive mutational analysis.

8. Functional modulation of a protein folding landscape via side-chain distortion.

9. Metamorphic proteins mediate evolutionary transitions of structure.

10. In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: implications for protein folding and assembly.