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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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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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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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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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Stabilization of protein structures
Current Opinion in Biotechnology, 1997The technique of protein stabilization has been improving steadily in recent years, but it is only in the past year or two that the stability of some protein molecules has been improved to the level of those from extreme thermophilic organisms. This was achieved by multiple mutations and often by utilizing the knowledge gained from the homologous ...
B, Lee, G, Vasmatzis
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Pressure Stability of Proteins
Annual Review of Physical Chemistry, 1993The stability of proteins toward temperature has been explored in much detail since the time that proteins were characterized as chemicals of constant composition, but the study of the effects of pressure upon pro teins is much more recent and has been much less frequent than that of temperature.
J L, Silva, G, Weber
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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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Archives of Biochemistry and Biophysics, 1973
Abstract The maximum melting points of 14 proteins in respect to pH are reported, the correlation coefficient between the hydrophobic index and the melting point was +0.622, and that between the average residue volumes and the melting points was +0.960.
H B, Bull, K, Breese
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Abstract The maximum melting points of 14 proteins in respect to pH are reported, the correlation coefficient between the hydrophobic index and the melting point was +0.622, and that between the average residue volumes and the melting points was +0.960.
H B, Bull, K, Breese
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Stabilization of Proteins for Storage
Cold Spring Harbor Protocols, 2010INTRODUCTIONFollowing isolation and purification, it is often necessary to store proteins and peptides for extended periods of time before performing detailed biophysical, enzymatic, and structural proteomics. Therefore, it is essential that the pure target protein maintain its original biological (or functional) behavior over an extended period of ...
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Destabilization and stabilization of proteins
Quarterly Reviews of Biophysics, 2005Introduction 351Part I. A succession of concepts 3521. Cooperativity 3522. Cosolvent interaction 3523. Linearity 3544. Solvent exchange 3545. Excluded volume 3566. Summation 357Part II 1. The Kirkwood–Buff approach 357Acknowledgments 360References 360In Part I the history of progress in the stabilization and destabilization of protein conformations by ...
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