Results 191 to 200 of about 321 (221)
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Thermodynamics of globular proteins
Journal of Biomolecular Structure and Dynamics, 2017The analysis of temperature-induced unfolding of proteins in aqueous solutions was performed. Based on the data of thermodynamic parameters of protein unfolding and using the method of semi-empirical calculations of hydration parameters at reference temperature 298 K, we obtained numerical values of enthalpy, free energy, and entropy which characterize
Nikolay N, Khechinashvili +3 more
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Synthesis of Globular Precursors
Chemistry – A European Journal, 2015Abstracto‐Carborane (C2B10H12) was adapted to perform as the core of globular macromolecules, dendrons or dendrimers. To meet this objective, precisely defined substitution patterns of terminal olefin groups on the carborane framework were subjected to Heck cross‐coupling reactions or hydroboration leading to hydroxyl terminated arms.
Teixidor, Francesc +5 more
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Science, 1984
In their attempt to reach kinetic equilibrium, through gravitational encounters between separate stars, globular clusters are driven to destruction, with their cores collapsing and their outer regions expanding. The effects of core collapse, which apparently produces x-ray sources, are not yet fully understood, but white dwarfs and neutron stars ...
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In their attempt to reach kinetic equilibrium, through gravitational encounters between separate stars, globular clusters are driven to destruction, with their cores collapsing and their outer regions expanding. The effects of core collapse, which apparently produces x-ray sources, are not yet fully understood, but white dwarfs and neutron stars ...
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Journal of Theoretical Biology, 1974
Abstract This paper inquires whether it is reasonable to expect the native structure of proteins to be “knotted”. To this end, some topological properties of polypeptides containing disulfide bridges are discussed using notions from mathematical knot theory and graph theory.
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Abstract This paper inquires whether it is reasonable to expect the native structure of proteins to be “knotted”. To this end, some topological properties of polypeptides containing disulfide bridges are discussed using notions from mathematical knot theory and graph theory.
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The absorption of globular proteins
Biopolymers, 1973AbstractA series of experiments is suggested to elucidate further the nature of the adsorption of globular proteins on polar solid surfaces. Two ratios of surface energies and the total protein volume are used to characterize the expected form of the adsorbed species. A simple model calculation illustrates the approach.
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Pediatric Neurology, 1999
Brainstem gliomas are a heterogeneous group of tumors whose prognosis and treatment depend not only on the histologic features but also on the location within the brainstem. Magnetic resonance imaging allows the recognition of a distinct type of brainstem glioma of the tectal region of the midbrain, leading to aqueductal compression and hydrocephalus ...
N L, Antunes, L, Tavora, M, Souweidane
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Brainstem gliomas are a heterogeneous group of tumors whose prognosis and treatment depend not only on the histologic features but also on the location within the brainstem. Magnetic resonance imaging allows the recognition of a distinct type of brainstem glioma of the tectal region of the midbrain, leading to aqueductal compression and hydrocephalus ...
N L, Antunes, L, Tavora, M, Souweidane
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Faraday Discussions of the Chemical Society, 1974
Globular proteins form gels as a result of aggregation to form strands followed by interaction of the strands to form the gel mesh. An approximate (pore size, concentration) relationship can be predicted from selected models of the aggregation process, which is consistent with that determined from electron micrographs of gels.
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Globular proteins form gels as a result of aggregation to form strands followed by interaction of the strands to form the gel mesh. An approximate (pore size, concentration) relationship can be predicted from selected models of the aggregation process, which is consistent with that determined from electron micrographs of gels.
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Conformational stability of globular proteins
Trends in Biochemical Sciences, 1990The conformational stability of ribonuclease T1 has been measured as a function of the variables of most interest to biochemists: temperature, pH, salt concentration, disulfide-bond content and amino acid sequence. The results provide insight into the forces that stabilize globular proteins.
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Enhancing stability of hybrid perovskite solar cells by imidazolium incorporation
Solar Energy Materials and Solar Cells, 2021Andrei Gabriel Tomulescu +2 more
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