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Kinetically controlled refolding of a heat-denatured hyperthermostable protein.
FEBS J. 2007 Nov; 274(22):5915-23.FJ

Abstract

The thermal denaturation of endo-beta-1,3-glucanase from the hyperthermophilic microorganism Pyrococcus furiosus was studied by calorimetry. The calorimetric profile revealed two transitions at 109 and 144 degrees C, corresponding to protein denaturation and complete unfolding, respectively, as shown by circular dichroism and fluorescence spectroscopy data. Calorimetric studies also showed that the denatured state did not refold to the native state unless the cooling temperature rate was very slow. Furthermore, previously denatured protein samples gave well-resolved denaturation transition peaks and showed enzymatic activity after 3 and 9 months of storage, indicating slow refolding to the native conformation over time.

Authors+Show Affiliations

Laboratory of Physical Chemistry and Colloid Science, Wageningen University, The Netherlands. sotiris@mit.eduNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17944946

Citation

Koutsopoulos, Sotirios, et al. "Kinetically Controlled Refolding of a Heat-denatured Hyperthermostable Protein." The FEBS Journal, vol. 274, no. 22, 2007, pp. 5915-23.
Koutsopoulos S, van der Oost J, Norde W. Kinetically controlled refolding of a heat-denatured hyperthermostable protein. FEBS J. 2007;274(22):5915-23.
Koutsopoulos, S., van der Oost, J., & Norde, W. (2007). Kinetically controlled refolding of a heat-denatured hyperthermostable protein. The FEBS Journal, 274(22), 5915-23.
Koutsopoulos S, van der Oost J, Norde W. Kinetically Controlled Refolding of a Heat-denatured Hyperthermostable Protein. FEBS J. 2007;274(22):5915-23. PubMed PMID: 17944946.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Kinetically controlled refolding of a heat-denatured hyperthermostable protein. AU - Koutsopoulos,Sotirios, AU - van der Oost,John, AU - Norde,Willem, Y1 - 2007/10/17/ PY - 2007/10/20/pubmed PY - 2008/1/30/medline PY - 2007/10/20/entrez SP - 5915 EP - 23 JF - The FEBS journal JO - FEBS J VL - 274 IS - 22 N2 - The thermal denaturation of endo-beta-1,3-glucanase from the hyperthermophilic microorganism Pyrococcus furiosus was studied by calorimetry. The calorimetric profile revealed two transitions at 109 and 144 degrees C, corresponding to protein denaturation and complete unfolding, respectively, as shown by circular dichroism and fluorescence spectroscopy data. Calorimetric studies also showed that the denatured state did not refold to the native state unless the cooling temperature rate was very slow. Furthermore, previously denatured protein samples gave well-resolved denaturation transition peaks and showed enzymatic activity after 3 and 9 months of storage, indicating slow refolding to the native conformation over time. SN - 1742-464X UR - https://www.unboundmedicine.com/medline/citation/17944946/Kinetically_controlled_refolding_of_a_heat_denatured_hyperthermostable_protein_ L2 - https://doi.org/10.1111/j.1742-4658.2007.06114.x DB - PRIME DP - Unbound Medicine ER -