The thermodynamic characteristics of complex formation between calcium ions and L-leucine in aqueous solution

Kurochkin, V Yu; Chernikov, V. V.; Orlova, T. D.

doi:10.1134/s0036024411040157

Cited by 4 publications

(2 citation statements)

References 10 publications

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“…In contrast, the pattern of ion coordination for the loop IV is changed, and particularly leucine at position 178 could play a role in metal binding. Its interaction is probably due to the π-polarization of the peptide group of leucine [21].…”

Section: Bioinformaticsmentioning

confidence: 99%

Site‐specific mutagenesis on Mnemiopsin 2: Calcium coordination and substrate binding properties of new variants

Ahmadi,

Jafarian,

Shirdel

2024

Luminescence

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We used site‐specific mutagenesis by targeting E179 and F190 on the structure of photoprotein Mnemiopsin 2 (Mn2) from Mnemiopsis leidyi. The tertiary structure of E179S and F190L mutants was made by the MODELLER program. Far‐ultraviolet circular dichroism data showed that the overall secondary structural content of photoprotein is not changed upon mutation, however the helicity and stabilizing interactions in helical structure decreases in mutants as compared with the wild‐type (WT) photoprotein. Fluorescence spectra data revealed that the tertiary structure of the mutants is more compact than that of WT Mn2. According to the heat‐induced denaturation experiments data, the melting temperature (Tm) for the unfolding of tertiary structure of the F190L variant increases by 3°C compared with that of the WT and E179S mutant. Interestingly, the conformational enthalpy of the F190L mutant (86 kcal mol−1) is considerably lower than those in the WT photoprotein (102 kcal mol−1) and E179S mutant (106 kcal mol−1). The significant difference in the enthalpy of the thermal unfolding process could be explained by considering that the thermally denatured state of the F190L mutant is structurally less expanded than the WT and E179S variants. Bioluminescence activity data showed that the maximum characteristic wavelengths of the mutants undergo blue shift as compared with the WT protein. Initial intensity of the F190L and E179S variants was recorded to be 137.5% and 55.9% of the WT protein, respectively.

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Section: Bioinformaticsmentioning

confidence: 99%

Site‐specific mutagenesis on Mnemiopsin 2: Calcium coordination and substrate binding properties of new variants

Ahmadi,

Jafarian,

Shirdel

2024

Luminescence

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“…Calcium is ubiquitous in all living organisms and performs a wide variety of essential biochemical processes, including glycolysis, cell signaling, ion transport, and apoptosis . Calcium-binding proteins (CaBPs) play a fundamental role in these processes and occur in eukarya, prokarya, and archaea. − The complexation of calcium to amino acid carboxylate groups has been observed in aqueous systems and may potentially occur in natural systems with elevated dissolved Ca 2+ concentrations. − The selection and concentration of such metal–ligand complexes at the mineral–water interfaces present within these environments could have led to the polymerization of primordial CaBPs as a crucial process in the emergence of complex biochemistry in early life.…”

Section: Introductionmentioning

confidence: 99%

Selective Adsorption of Aspartate Facilitated by Calcium on Brucite [Mg(OH)₂]

Estrada

Sverjensky

Hazen

2018

ACS Earth Space Chem.

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Dissolved ions present in an aqueous environment may significantly improve biomolecule attachment at mineral surfaces through the formation of cooperative surface complexes. To test whether this phenomenon results in the selective adsorption of an organic species, we conducted batch adsorption experiments with an equimolar mixture of the amino acids aspartate, glycine, lysine, leucine, and phenylalanine onto powdered brucite [Mg(OH) 2 ] at pH 10.2. We performed the batch experiments in triplicate both without and with 4.1 mM CaCl 2 . In experiments without CaCl 2 , we observed that up to 0.7 μmol m −2 of aspartate and about 0.4 μmol m −2 each of the remaining four amino acids adsorbed onto brucite. When we added CaCl 2 , we found that up to 1.6 μmol m −2 of aspartate selectively adsorbed onto the brucite surface relative to between 0.2 and 0.3 μmol m −2 of the other amino acids. We measured the brucite particle surface charge to be slightly positive without added CaCl 2 , but the surface charge becomes significantly more positive in the presence of CaCl 2 . Our results suggest that negatively charged molecules selectively and cooperatively adsorb onto brucite when CaCl 2 is added to the system. This study emphasizes the importance of the dissolved ionic profile of a geochemical environment when evaluating the role of mineral surfaces in the evolution of prebiotic chemistry. The presence of dissolved ions at a mineral−water interface can selectively enhance the adsorption and concentration of specific molecules, which may serve as a key process in molecular self-organization and the assembly of proteins that are composed of metal−ligand complexes.

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A Quantum Chemical Simulation of the Interaction Between Leucine and the Dimer of Sodium Dodecyl Sulphate

et al. 2018

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The thermodynamic characteristics of complex formation between calcium ions and L-leucine in aqueous solution

Cited by 4 publications

References 10 publications

Site‐specific mutagenesis on Mnemiopsin 2: Calcium coordination and substrate binding properties of new variants

Site‐specific mutagenesis on Mnemiopsin 2: Calcium coordination and substrate binding properties of new variants

Selective Adsorption of Aspartate Facilitated by Calcium on Brucite [Mg(OH)₂]

A Quantum Chemical Simulation of the Interaction Between Leucine and the Dimer of Sodium Dodecyl Sulphate

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The thermodynamic characteristics of complex formation between calcium ions and L-leucine in aqueous solution

Cited by 4 publications

References 10 publications

Site‐specific mutagenesis on Mnemiopsin 2: Calcium coordination and substrate binding properties of new variants

Site‐specific mutagenesis on Mnemiopsin 2: Calcium coordination and substrate binding properties of new variants

Selective Adsorption of Aspartate Facilitated by Calcium on Brucite [Mg(OH)2]

A Quantum Chemical Simulation of the Interaction Between Leucine and the Dimer of Sodium Dodecyl Sulphate

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Product

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Selective Adsorption of Aspartate Facilitated by Calcium on Brucite [Mg(OH)₂]