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Thermal unfolding of calreticulin. Structural and thermodynamic characterization of the transition
(Elsevier Science, 2019-03)
Calreticulin (CRT) is a calcium-binding protein that participates in several cellular processes including the control of protein folding and homeostasis of Ca2+. Its folding, stability and functions are strongly controlled ...
β-Galactosidase at the membrane–water interface: a case of an active enzyme with non-native conformation
(Elsevier Science, 2013-02)
Previously we demonstrated that Escherichia coli beta-galactosidase (β-Gal) binds to zwitterionic lipid membranes improving its catalytic activity. To understand the activation mechanism from the protein perspective, here ...
The thermal unfolding of beta 2-Glycoprotein
(2013)
Beta 2- Glycoprotein I (B2GPI) is an abundant glycoprotein of human plasma. It participates in blood coagulation processes and the clearance of phosphatidylserine exposing- apoptotic cells. B2GPI is also the major antigen ...
Kinetic stability of membrane proteins
(Springer Verlag, 2017-10)
Although membrane proteins constitute an important class of biomolecules involved in key cellular processes, study of the thermodynamic and kinetic stability of their structures is far behind that of soluble proteins. It ...
Desnaturalización térmica de la β-galactosidasa de Kluyveromyces lactis
(Universidad Autónoma Metropolitana (México). Unidad Azcapotzalco. División de Ciencias Básicas e Ingeniería., 2017)
En este trabajo se estudió por dicroísmo circular, una técnica espectroscópica, la desnaturalización térmica de la β-galactosidasa de Kluyveromices lactis, una enzima dimérica, para establecer un posible mecanismo de ...
Methionine adenosyltransferase α-helix structure unfolds at lower temperatures than β-sheet: A 2D-IR study
(Cell Press, 2004-12)
Two-dimensional infrared spectroscopy has been used to characterize rat liver methionine adenosyltransferase and the events taking place during its thermal unfolding. Secondary structure data have been obtained for the ...
The stability and aggregation properties of the GTPase domain from human SEPT4
(ELSEVIER SCIENCE BV, 2008)
The septins are a family of conserved proteins involved in cytokinesis and cortical organization. An increasing amount of data implicates different septins in diverse pathological conditions including neurodegenerative ...
Thermal stability of CopA, a polytopic membrane protein from the hyperthermophile Archaeoglobus fulgidus
(Elsevier Science Inc., 2008-03)
Despite recent progress in understanding membrane protein folding, little is known about the mechanisms stabilizing these proteins. Here we characterize the kinetic thermal stability of CopA, a thermophilic P(IB)-type ...
Expression, purification and spectroscopic analysis of an HdrC: An iron-sulfur cluster-containing protein from Acidithiobacillus ferrooxidans
(Elsevier B.V., 2011-06-01)
Iron-sulfur cluster-containing proteins are present in all living organisms and are considered to be very ancient due to their ubiquity on the three domains of life, their importance in anaerobic metabolic pathways and ...
Expression, purification and spectroscopic analysis of an HdrC: An iron-sulfur cluster-containing protein from Acidithiobacillus ferrooxidans
(Elsevier B.V., 2011-06-01)
Iron-sulfur cluster-containing proteins are present in all living organisms and are considered to be very ancient due to their ubiquity on the three domains of life, their importance in anaerobic metabolic pathways and ...