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Biophysical characterization of Gir2, a highly acidic protein of Saccharomyces cerevisiae with anomalous electrophoretic behavior
(Elsevier B.V., 2004-01-30)
Gir2 is an uncharacterized protein of Saccharomyces cerevisiae, containing a RWD/GI domain. in this work, we report the biophysical characterization of Gir2. His-tagged Gir2, expressed and purified from Escherichia coli, ...
Unfolding pathway of the dimeric and tetrameric forms of phosphofructokinase-2 from Escherichia coli
(2007)
Escherichia coli phosphofructokinase-2 (Pfk-2) is an oligomeric enzyme characterized by two kinds of interfaces: a monomer-monomer interface, critical for enzymatic activity, and a dimer-dimer interface formed upon ...
Global Implications of Local Unfolding Phenomena, Probed by Cysteine Reactivity in Human Frataxin
(Nature Publishing Group, 2019-12)
Local events that affect specific regions of proteins are of utmost relevance for stability and function. The aim of this study is to quantitatively assess the importance of locally-focused dynamics by means of a simple ...
Human FEZ1 Protein Forms a Disulfide Bond Mediated Dimer: Implications for Cargo Transport
(Amer Chemical SocWashingtonEUA, 2010)
Thermodynamic model for the analysis of calorimetric data of oligomeric proteins
(American Chemical Society, 2008-12)
The thermodynamic parameters for the process of protein unfolding can be obtained through differential scanning calorimetry. However, the unfolding process may not be a two-state one. Between the native and the unfolded ...
Reversible Unfolding of a Thermophilic Membrane Protein in Phospholipid/Detergent Mixed Micelles
(Academic Press Ltd - Elsevier Science Ltd, 2010-03)
Folding mechanisms and stability of membrane proteins are poorly understood because of the known difficulties in finding experimental conditions under which reversible denaturation could be possible. In this work, we ...
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 ...
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 ...
Frustration and hydrophobicity interplay in protein folding and protein evolution
(American Institute of Physics (AIP), 2006-08-28)
A lattice model is used to study mutations and compacting effects on protein folding rates and folding temperature. In the context of protein evolution, we address the question regarding the best scenario for a polypeptide ...
Frustration and hydrophobicity interplay in protein folding and protein evolution
(American Institute of Physics (AIP), 2006-08-28)
A lattice model is used to study mutations and compacting effects on protein folding rates and folding temperature. In the context of protein evolution, we address the question regarding the best scenario for a polypeptide ...