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Pure Appl. Chem., 1994, Vol. 66, No. 3, pp. 485-489

http://dx.doi.org/10.1351/pac199466030485

Life in the pressure cooker: The thermal unfolding of proteins from hyperthermophiles

H. H. Klump, M. W. W. Adams and F. T. Robb

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  • Lazaridis Themis, Lee Irwin, Karplus Martin: Dynamics and unfolding pathways of a hyperthermophilic and a mesophilic rubredoxin. Protein Sci 2008, 6, 2589. <http://dx.doi.org/10.1002/pro.5560061211>
  • De La Cruz Aida Flor A., Dahlquist Fredrick W., James Remington S., Swanson Ronald V., Simon Melvin I., Usher Ken C.: Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability. Protein Sci 2008, 7, 403. <http://dx.doi.org/10.1002/pro.5560070221>
  • Koutsopoulos Sotirios, van der Oost John, Norde Willem: Kinetically controlled refolding of a heat-denatured hyperthermostable protein : Kinetically controlled refolding of a denatured protein. FEBS J 2007, 274, 5915. <http://dx.doi.org/10.1111/j.1742-4658.2007.06114.x>
  • Imai Takeo, Yasujima Daisuke, Siddiqui Masood Ahmed: An instant measurement of oxidoreductase activity above 100°C by monitoring the absorbance change. J Biosci Bioengin 2004, 97, 336. <http://dx.doi.org/10.1016/S1389-1723(04)70215-7>
  • IMAI TAKEO, YASUJIMA DAISUKE, SIDDIQUI MASOOD AHMED: An Instant Measurement of Oxidoreductase Activity above 100°C by Monitoring the Absorbance Change. J BIOSCI BIOENG 2004, 97, 336. <http://dx.doi.org/10.1263/jbb.97.336>
  • Ogasahara Kyoko, Khechinashvili Nikolay N., Nakamura Mamoru, Yoshimoto Tadashi, Yutani Katsuhide: Thermal stability of pyrrolidone carboxyl peptidases from the hyperthermophilic Archaeon, Pyrococcus furiosus. European Journal of Biochemistry 2001, 268, 3233. <http://dx.doi.org/10.1046/j.1432-1327.2001.02220.x>
  • Bonomi Francesco, Iametti Stefania, Mazzini Stefania, Fessas Dimitrios, Kurtz Donald M.: Thermal stability of Clostridium pasteurianum rubredoxin: Deconvoluting the contributions of the metal site and the protein. Protein Sci 2000, 9, 2413. <http://dx.doi.org/10.1110/ps.9.12.2413>
  • Middaugh C Russell, Edwards Karen-Leigh T: Recent advances in our understanding of protein conformational stability from a pharmaceutical perspective. Expert Opin Invest Drugs 1998, 7, 1493. <http://dx.doi.org/10.1517/13543784.7.9.1493>
  • Knapp Stefan, de Vos Willem M, Rice David, Ladenstein Rudolf: Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0 Å resolution. Journal of Molecular Biology 1997, 267, 916. <http://dx.doi.org/10.1006/jmbi.1996.0900>
  • Hiller R., Zhou Z. H., Adams M. W. W., Englander S. W.: Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200 C. Proceedings of the National Academy of Sciences 1997, 94, 11329. <http://dx.doi.org/10.1073/pnas.94.21.11329>
  • Rees Douglas C, Adams Michael WW: Hyperthermophiles: taking the heat and loving it. Struct Fold Des 1995, 3, 251. <http://dx.doi.org/10.1016/S0969-2126(01)00155-1>
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