Linking the Structure and Thermal Stability of β-Galactoside-Binding Protein Galectin-1 to Ligand Binding and Dimerization Equilibria

Biochemistry ◽  
2010 ◽  
Vol 49 (35) ◽  
pp. 7652-7658 ◽  
Author(s):  
Santiago Di Lella ◽  
Marcelo A. Martí ◽  
Diego O. Croci ◽  
Carlos M. A. Guardia ◽  
Juan C. Díaz-Ricci ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Ligand Binding ◽  
Binding Protein ◽  
Thermal Stability Of

Chemical and Thermal Stability of Insulin: Effects of Zinc and Ligand Binding to the Insulin Zinc-Hexamer

2006 ◽  
Vol 23 (11) ◽  
pp. 2611-2620 ◽  
Author(s):  
Kasper Huus ◽  
Svend Havelund ◽  
Helle B. Olsen ◽  
Marco van de Weert ◽  
Sven Frokjaer
Keyword(s):  
Thermal Stability ◽  
Ligand Binding ◽  
Thermal Stability Of

scholarly journals Experimental Insight into the Structural and Functional Roles of the ‘Black’ and ‘Gray’ Clusters in Recoverin, a Calcium Binding Protein with Four EF-Hand Motifs

Molecules ◽  
2019 ◽  
Vol 24 (13) ◽  
pp. 2494
Author(s):  
Sergey E. Permyakov ◽  
Alisa S. Vologzhannikova ◽  
Ekaterina L. Nemashkalova ◽  
Alexei S. Kazakov ◽  
Alexander I. Denesyuk ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Amino Acids ◽  
Calcium Binding ◽  
Binding Protein ◽  
Critical Role ◽  
Binding Motif ◽  
Terminal Domain ◽  
Ef Hand ◽  
Helical Content ◽  
Thermal Stability Of

Recently, we have found that calcium binding proteins of the EF-hand superfamily (i.e., a large family of proteins containing helix-loop-helix calcium binding motif or EF-hand) contain two types of conserved clusters called cluster I (‘black’ cluster) and cluster II (‘grey’ cluster), which provide a supporting scaffold for the Ca2+ binding loops and contribute to the hydrophobic core of the EF-hand domains. Cluster I is more conservative and mostly incorporates aromatic amino acids, whereas cluster II includes a mix of aromatic, hydrophobic, and polar amino acids of different sizes. Recoverin is EF-hand Ca2+-binding protein containing two ‘black’ clusters comprised of F35, F83, Y86 (N-terminal domain) and F106, E169, F172 (C-terminal domain) as well as two ‘gray’ clusters comprised of F70, Q46, F49 (N-terminal domain) and W156, K119, V122 (C-terminal domain). To understand a role of these residues in structure and function of human recoverin, we sequentially substituted them for alanine and studied the resulting mutants by a set of biophysical methods. Under metal-free conditions, the ‘black’ clusters mutants (except for F35A and E169A) were characterized by an increase in the α-helical content, whereas the ‘gray’ cluster mutants (except for K119A) exhibited the opposite behavior. By contrast, in Ca2+-loaded mutants the α-helical content was always elevated. In the absence of calcium, the substitutions only slightly affected multimerization of recoverin regardless of their localization (except for K119A). Meanwhile, in the presence of calcium mutations in N-terminal domain of the protein significantly suppressed this process, indicating that surface properties of Ca2+-bound recoverin are highly affected by N-terminal cluster residues. The substitutions in C-terminal clusters generally reduced thermal stability of recoverin with F172A (‘black’ cluster) as well as W156A and K119A (‘gray’ cluster) being the most efficacious in this respect. In contrast, the mutations in the N-terminal clusters caused less pronounced differently directed changes in thermal stability of the protein. The substitutions of F172, W156, and K119 in C-terminal domain of recoverin together with substitution of Q46 in its N-terminal domain provoked significant but diverse changes in free energy associated with Ca2+ binding to the protein: the mutant K119A demonstrated significantly improved calcium binding, whereas F172A and W156A showed decrease in the calcium affinity and Q46A exhibited no ion coordination in one of the Ca2+-binding sites. The most of the N-terminal clusters mutations suppressed membrane binding of recoverin and its inhibitory activity towards rhodopsin kinase (GRK1). Surprisingly, the mutant W156A aberrantly activated rhodopsin phosphorylation regardless of the presence of calcium. Taken together, these data confirm the scaffolding function of several cluster-forming residues and point to their critical role in supporting physiological activity of recoverin.

The Ordered Phase Formation in Ti-Al-Ga Alloys

1970 ◽  
Vol 28 ◽  
pp. 440-441
Author(s):  
Shiro Fujishiro ◽  
Harold L. Gegel
Keyword(s):  
Thermal Stability ◽  
High Temperature ◽  
Titanium Alloys ◽  
Growth Kinetics ◽  
Stoichiometric Composition ◽  
Good Potential ◽  
Alpha Titanium ◽  
Cold Rolled ◽  
Kinetics Of ◽  
Thermal Stability Of

Ordered-alpha titanium alloys having a DO19 type structure have good potential for high temperature (600°C) applications, due to the thermal stability of the ordered phase and the inherent resistance to recrystallization of these alloys. Five different Ti-Al-Ga alloys consisting of equal atomic percents of aluminum and gallium solute additions up to the stoichiometric composition, Ti3(Al, Ga), were used to study the growth kinetics of the ordered phase and the nature of its interface.The alloys were homogenized in the beta region in a vacuum of about 5×10-7 torr, furnace cooled; reheated in air to 50°C below the alpha transus for hot working. The alloys were subsequently acid cleaned, annealed in vacuo, and cold rolled to about. 050 inch prior to additional homogenization

Microstructure studies of tungsten silicide schottky contacts on Gaas

1987 ◽  
Vol 45 ◽  
pp. 328-329
Author(s):  
Yih-Cheng Shih ◽  
E. L. Wilkie
Keyword(s):  
Thermal Stability ◽  
Field Effect Transistors ◽  
Schottky Contact ◽  
Schottky Contacts ◽  
Excellent Thermal Stability ◽  
Barrier Heights ◽  
Gaas Substrates ◽  
Film Adhesion ◽  
Threshold Voltages ◽  
Thermal Stability Of

Tungsten silicides (WSix) have been successfully used as the gate materials in self-aligned GaAs metal-semiconductor-field- effect transistors (MESFET). Thermal stability of the WSix/GaAs Schottky contact is of major concern since the n+ implanted source/drain regions must be annealed at high temperatures (∼ 800°C). WSi0.6 was considered the best composition to achieve good device performance due to its low stress and excellent thermal stability of the WSix/GaAs interface. The film adhesion and the uniformity in barrier heights and ideality factors of the WSi0.6 films have been improved by depositing a thin layer of pure W as the first layer on GaAs prior to WSi0.6 deposition. Recently WSi0.1 has been used successfully as the gate material in 1x10 μm GaAs FET's on the GaAs substrates which were sputter-cleaned prior to deposition. These GaAs FET's exhibited uniform threshold voltages across a 51 mm wafer with good film adhesion after annealing at 800°C for 10 min.

Thermal stability of Al-Cu-Fe icosahedral alloys

1991 ◽  
Vol 1 (12) ◽  
pp. 1823-1836 ◽  
Author(s):  
M. Bessière ◽  
A. Quivy ◽  
S. Lefebvre ◽  
J. Devaud-Rzepski ◽  
Y. Calvayrac
Keyword(s):  
Thermal Stability ◽  
Thermal Stability Of

Practical criteria for the thermal stability of a unidimensional superconductor

1994 ◽  
Vol 4 (4) ◽  
pp. 653-657
Author(s):  
B. Bonzi ◽  
M. El Khomssi ◽  
H. Lanchon-Ducauquis
Keyword(s):  
Thermal Stability ◽  
Thermal Stability Of

Time and thermal stability of magnetic properties of amorphous Fe80TM3B17 alloys

1998 ◽  
Vol 08 (PR2) ◽  
pp. Pr2-63-Pr2-66 ◽  
Author(s):  
R. Varga ◽  
P. Vojtaník ◽  
A. Lovas
Keyword(s):  
Thermal Stability ◽  
Magnetic Properties ◽  
Thermal Stability Of
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