Thermodynamic and kinetic stability of a large multi-domain enzyme from the hyperthermophile Aeropyrum pernix-Reference-Cited by-同舟云学术

Thermodynamic and kinetic stability of a large multi-domain enzyme from the hyperthermophile Aeropyrum pernix

Published:2010-01-08 Issue:2 Volume:14 Page:213-223
ISSN:1431-0651
Container-title:Extremophiles
language:en
Short-container-title:Extremophiles

Author:

Karlström Mikael,Chiaraluce Roberta,Giangiacomo Laura,Steen Ida Helene,Birkeland Nils-Kåre,Ladenstein Rudolf,Consalvi Valerio

Publisher

Springer Science and Business Media LLC

Subject

Molecular Medicine,General Medicine,Microbiology

Link

http://link.springer.com/content/pdf/10.1007/s00792-009-0300-0.pdf

Reference51 articles.

1. Anderson DE, Becktel WJ, Dahlquist FW (1990) pH-induced denaturation of proteins: a single salt bridge contributes 3–5 kcal/mol to the free energy of folding of T4 lysozyme. Biochemistry 29:2403–2408

2. Baker D, Agard DA (1994) Kinetics versus thermodynamics in protein folding. Biochemistry 33:7505–7509

3. Baskakov IV, Legname G, Gryczynski Z, Prusiner SB (2004) The peculiar nature of unfolding of the human prion protein. Protein Sci 13:586–595

4. Benitez-Cardoza CG, Rojo-Dominguez A, Hernandez-Arana A (2001) Temperature-induced denaturation and renaturation of triosephosphate isomerase from Saccharomyces cerevisiae: evidence of dimerization coupled to refolding of the thermally unfolded protein. Biochemistry 40:9049–9058

5. Bieri O, Kiefhaber T (2000) Kinetic models in protein folding. In: Pain RH (ed) Mechanisms of protein folding, 2nd edn. Oxford University Press, Oxford

Cited by 2 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. A Brief History of Colour, the Environmental Impact of Synthetic Dyes and Removal by Using Laccases;Molecules;2021-06-22

2. Optimization of Laccase Fermentation and Evaluation of Kinetic and Thermodynamic Parameters of a Partially Purified Laccase Produced byDaedalea flavida;Preparative Biochemistry and Biotechnology;2014-09-25