Results 251 to 260 of about 6,635,393 (306)
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Cellular and Molecular Life Sciences, 1997
The stabilization of proteins is discussed from the theoretical and practical points of view. Methods are described for kinetic stabilization and protection from deterioration, as well as the thermodynamic stabilization of proteins.
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The stabilization of proteins is discussed from the theoretical and practical points of view. Methods are described for kinetic stabilization and protection from deterioration, as well as the thermodynamic stabilization of proteins.
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Protein crystals and their stability
Journal of Crystal Growth, 1992Assuming a simple model, it can be derived that the free energy difference between protein molecules in the crystalline state and in a saturated solution is determined by C(sol)/C(cr), in which C(sol) is the concentration of the protein in the solution and C(cr) that in the crystal.
DRENTH, J, HAAS, C
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THE THERMODYNAMIC STABILITY OF PROTEINS
Annual Review of Biophysics and Biophysical Chemistry, 1987BINDING AND THE SELECTIVE INTERACTION OF PROTEINS 121 Stoichiometr ic Binding 122 Ther modynamic Binding 123 What Do We Learn/rom Exp eriment? 128 TRANSITION THERMODYNAMICS AS A PROBE OF PERTURBATIONS .
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Stability and stabilization of globular proteins in solution
Journal of Biotechnology, 2000Proteins are multifunctional: their amino acid sequences simultaneously determine folding, function and turnover. Correspondingly, evolution selected for compromises between rigidity (stability) and flexibility (folding/function/degradation), to the result that generally the free energy of stabilization of globular proteins in solution is the ...
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Stability of Tethered Proteins
Langmuir, 2009The stability of tethered globular proteins under denaturing conditions was interrogated with a hydrophobic surface, since conventional structural methods like circular dichroism (CD) and fluorescence or infrared spectroscopy could not be used because of the presence of an opaque solid substrate and extremely low surface concentrations.
Gaurav, Anand +3 more
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Stability of Protein Pharmaceuticals
Pharmaceutical Research, 1989Recombinant DNA technology has now made it possible to produce proteins for pharmaceutical applications. Consequently, proteins produced via biotechnology now comprise a significant portion of the drugs currently under development. Isolation, purification, formulation, and delivery of proteins represent significant challenges to pharmaceutical ...
M C, Manning, K, Patel, R T, Borchardt
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Trehalose and Protein Stability
Current Protocols in Protein Science, 2010AbstractThe role of osmolytes, and especially trehalose, in stabilizing proteins under stress conditions is now a widely accepted fact. The physical and chemical properties of trehalose, i.e., low chemical reactivity, nonreducing nature, high glass transition temperature, high affinity for water molecules, existence of a number of polymorphs, etc ...
Nishant Kumar, Jain, Ipsita, Roy
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Biopolymers, 1987
AbstractThe stability curve of a protein is defined as the plot of the free energy of unfolding as a function of temperature. For most proteins the change in heat capacity on denaturation, or unfolding, is large but approximately constant. When unfolding is s two‐state process, most of the salient features of the stability curves of proteins can be ...
W J, Becktel, J A, Schellman
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AbstractThe stability curve of a protein is defined as the plot of the free energy of unfolding as a function of temperature. For most proteins the change in heat capacity on denaturation, or unfolding, is large but approximately constant. When unfolding is s two‐state process, most of the salient features of the stability curves of proteins can be ...
W J, Becktel, J A, Schellman
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2020
Proteins, in general, fold to a well-organized three-dimensional structure in order to function. The stability of this functional shape can be perturbed by external environmental conditions, such as temperature. Understanding the molecular factors underlying the resistance of proteins to the thermal stress has important consequences.
Sterpone, Fabio +2 more
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Proteins, in general, fold to a well-organized three-dimensional structure in order to function. The stability of this functional shape can be perturbed by external environmental conditions, such as temperature. Understanding the molecular factors underlying the resistance of proteins to the thermal stress has important consequences.
Sterpone, Fabio +2 more
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Mechanical stability of proteins
The Journal of Chemical Physics, 2009A number of experiments and experimentally based simulations showed that β-proteins are mechanically more stable than α-proteins. However, the theory that might explain this evidence is still lacking. In this paper we have developed a simple elastic theory, which allows to estimate critical forces for stretching both kinds of proteins.
A M, Gabovich, Mai Suan, Li
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