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.
Links
MeSH
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 -