Role of chemical potential in relaxation of faceted crystal structure

2014 ◽  
Vol 89 (6) ◽  
Author(s):  
Joshua P. Schneider ◽  
Kanna Nakamura ◽  
Dionisios Margetis
Keyword(s):  
Crystal Structure ◽  
Chemical Potential

scholarly journals Role of Chemistry and Crystal Structure on the Electronic Defect States in Cs-Based Halide Perovskites

Materials ◽  
2021 ◽  
Vol 14 (4) ◽  
pp. 1032
Author(s):  
Anirban Naskar ◽  
Rabi Khanal ◽  
Samrat Choudhury
Keyword(s):  
Crystal Structure ◽  
Density Functional ◽  
Covalent Bond ◽  
Density Functional Theory Calculations ◽  
Antisite Defect ◽  
Defect States ◽  
Functional Theory ◽  
Electronic Defect ◽  
Constituent Elements

The electronic structure of a series perovskites ABX3 (A = Cs; B = Ca, Sr, and Ba; X = F, Cl, Br, and I) in the presence and absence of antisite defect XB were systematically investigated based on density-functional-theory calculations. Both cubic and orthorhombic perovskites were considered. It was observed that for certain perovskite compositions and crystal structure, presence of antisite point defect leads to the formation of electronic defect state(s) within the band gap. We showed that both the type of electronic defect states and their individual energy level location within the bandgap can be predicted based on easily available intrinsic properties of the constituent elements, such as the bond-dissociation energy of the B–X and X–X bond, the X–X covalent bond length, and the atomic size of halide (X) as well as structural characteristic such as B–X–B bond angle. Overall, this work provides a science-based generic principle to design the electronic states within the band structure in Cs-based perovskites in presence of point defects such as antisite defect.

scholarly journals Crystal structures of Ca2+–calmodulin bound to NaV C-terminal regions suggest role for EF-hand domain in binding and inactivation

2019 ◽  
Vol 116 (22) ◽  
pp. 10763-10772 ◽  
Author(s):  
Bernd R. Gardill ◽  
Ricardo E. Rivera-Acevedo ◽  
Ching-Chieh Tung ◽  
Filip Van Petegem
Keyword(s):  
Crystal Structure ◽  
Binding Sites ◽  
Binding Mode ◽  
Conformational Switch ◽  
Channel Inactivation ◽  
Dependent Inactivation ◽  
Ef Hand ◽  
Inherited Arrhythmia ◽  
A Site

Voltage-gated sodium (NaV) and calcium channels (CaV) form targets for calmodulin (CaM), which affects channel inactivation properties. A major interaction site for CaM resides in the C-terminal (CT) region, consisting of an IQ domain downstream of an EF-hand domain. We present a crystal structure of fully Ca2+-occupied CaM, bound to the CT of NaV1.5. The structure shows that the C-terminal lobe binds to a site ∼90° rotated relative to a previous site reported for an apoCaM complex with the NaV1.5 CT and for ternary complexes containing fibroblast growth factor homologous factors (FHF). We show that the binding of FHFs forces the EF-hand domain in a conformation that does not allow binding of the Ca2+-occupied C-lobe of CaM. These observations highlight the central role of the EF-hand domain in modulating the binding mode of CaM. The binding sites for Ca2+-free and Ca2+-occupied CaM contain targets for mutations linked to long-QT syndrome, a type of inherited arrhythmia. The related NaV1.4 channel has been shown to undergo Ca2+-dependent inactivation (CDI) akin to CaVs. We present a crystal structure of Ca2+/CaM bound to the NaV1.4 IQ domain, which shows a binding mode that would clash with the EF-hand domain. We postulate the relative reorientation of the EF-hand domain and the IQ domain as a possible conformational switch that underlies CDI.

scholarly journals Spotlight on Alkali Metals: The Structural Chemistry of Alkali Metal Thallides

Crystals ◽  
2020 ◽  
Vol 10 (11) ◽  
pp. 1013
Author(s):  
Stefanie Gärtner
Keyword(s):  
Crystal Structure ◽  
Alkali Metal ◽  
Crystal Structures ◽  
Alkali Metals ◽  
Valence Electron ◽  
Oxidation States ◽  
Valence Electron Concentration ◽  
Base Metals ◽  
Charge Balancing

Alkali metal thallides go back to the investigative works of Eduard Zintl about base metals in negative oxidation states. In 1932, he described the crystal structure of NaTl as the first representative for this class of compounds. Since then, a bunch of versatile crystal structures has been reported for thallium as electronegative element in intermetallic solid state compounds. For combinations of thallium with alkali metals as electropositive counterparts, a broad range of different unique structure types has been observed. Interestingly, various thallium substructures at the same or very similar valence electron concentration (VEC) are obtained. This in return emphasizes that the role of the alkali metals on structure formation goes far beyond ancillary filling atoms, which are present only due to charge balancing reasons. In this review, the alkali metals are in focus and the local surroundings of the latter are discussed in terms of their crystallographic sites in the corresponding crystal structures.

Role of electronic factors in the formation of anionic complexes of tellurium(IV): Crystal structure of bis(4-methylbenzoylmethyltriphenylphosphonium) hexabromotellurate(IV)

Polyhedron ◽  
2006 ◽  
Vol 25 (3) ◽  
pp. 747-752
Author(s):  
Ashok K.S. Chauhan ◽  
Arun Kumar ◽  
Shobhit Charan ◽  
Ramesh C. Srivastava ◽  
Ray J. Butcher
Keyword(s):  
Crystal Structure ◽  
Anionic Complexes

Crystal Structure of Type 1 Ribonuclease H from Hyperthermophilic ArchaeonSulfolobus tokodaii:  Role of Arginine 118 and C-Terminal Anchoring†,‡

Biochemistry ◽  
2007 ◽  
Vol 46 (41) ◽  
pp. 11494-11503 ◽  
Author(s):  
Dong-Ju You ◽  
Hyongi Chon ◽  
Yuichi Koga ◽  
Kazufumi Takano ◽  
Shigenori Kanaya
Keyword(s):  
Crystal Structure ◽  
Ribonuclease H

Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism

2001 ◽  
Vol 359 (1) ◽  
pp. 65-75 ◽  
Author(s):  
Valeria MENCHISE ◽  
Catherine CORBIER ◽  
Claude DIDIERJEAN ◽  
Michele SAVIANO ◽  
Ettore BENEDETTI ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Proton Transfer ◽  
Chlamydomonas Reinhardtii ◽  
Catalytic Mechanism ◽  
Structural Data ◽  
Careful Analysis ◽  
Wild Type ◽  
Thioredoxin H ◽  
Dynamics Simulations

Thioredoxins are ubiquitous proteins which catalyse the reduction of disulphide bridges on target proteins. The catalytic mechanism proceeds via a mixed disulphide intermediate whose breakdown should be enhanced by the involvement of a conserved buried residue, Asp-30, as a base catalyst towards residue Cys-39. We report here the crystal structure of wild-type and D30A mutant thioredoxin h from Chlamydomonas reinhardtii, which constitutes the first crystal structure of a cytosolic thioredoxin isolated from a eukaryotic plant organism. The role of residue Asp-30 in catalysis has been revisited since the distance between the carboxylate OD1 of Asp-30 and the sulphur SG of Cys-39 is too great to support the hypothesis of direct proton transfer. A careful analysis of all available crystal structures reveals that the relative positioning of residues Asp-30 and Cys-39 as well as hydrophobic contacts in the vicinity of residue Asp-30 do not allow a conformational change sufficient to bring the two residues close enough for a direct proton transfer. This suggests that protonation/deprotonation of Cys-39 should be mediated by a water molecule. Molecular-dynamics simulations, carried out either in vacuo or in water, as well as proton-inventory experiments, support this hypothesis. The results are discussed with respect to biochemical and structural data.

Noncommutative scalar field in de Sitter space–time and pair creation process

2021 ◽  
Vol 36 (02) ◽  
pp. 2150011
Author(s):  
Nabil Mehdaoui ◽  
Lamine Khodja ◽  
Salah Haouat
Keyword(s):  
Scalar Field ◽  
Chemical Potential ◽  
De Sitter Space ◽  
Space Time ◽  
Pair Creation ◽  
De Sitter ◽  
Creation Process ◽  
Scalar Particles ◽  
Constant Electromagnetic Field

In this work, we address the process of pair creation of scalar particles in [Formula: see text] de Sitter space–time in presence of a constant electromagnetic field by applying the noncommutativity on the scalar field up to first-order in [Formula: see text]. We calculate the density of particles created in the vacuum by the mean of the Bogoliubov transformations. In contrast to a previous result, we show that noncommutativity contributes to the pair creation process. We find that the noncommutativity plays the same role of chemical potential and gives an important interest for studies at high energies.

scholarly journals The crystal structure of Mycobacterium tuberculosis high-temperature requirement A protein reveals an autoregulatory mechanism

2018 ◽  
Vol 74 (12) ◽  
pp. 803-809
Author(s):  
Arvind Kumar Gupta ◽  
Debashree Behera ◽  
Balasubramanian Gopal
Keyword(s):  
Crystal Structure ◽  
Mycobacterium Tuberculosis ◽  
High Temperature ◽  
Catalytic Domain ◽  
Pdz Domain ◽  
Regulatory Pathways ◽  
Inactive Conformation ◽  
Temperature Requirement ◽  
Autoregulatory Mechanism

The crystal structure of Mycobacterium tuberculosis high-temperature requirement A (HtrA) protein was determined at 1.83 Å resolution. This membrane-associated protease is essential for the survival of M. tuberculosis. The crystal structure reveals that interactions between the PDZ domain and the catalytic domain in HtrA lead to an inactive conformation. This finding is consistent with its proposed role as a regulatory protease that is conditionally activated upon appropriate environmental triggers. The structure provides a basis for directed studies to evaluate the role of this essential protein and the regulatory pathways that are influenced by this protease.

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