A simple spin system is studied as an analog for proteins. We investigate how the introduction of randomness and frustration into the system affects the designability and stability of ground-state configurations. We observe that the spin system exhibits proteinlike behavior in the vicinity of the transition between a ferromagnet and a spin glass. Our results illuminate some guiding principles in protein evolution. © 2001 The American Physical Society
Statistical thermodynamics of protein solutions is often studied in terms of simple, microscopic mod...
Proteins are the common constituents of all living cells. They are molecular machines that interact ...
Protein functions require conformational motions. We show here that the dominant conformational moti...
We explicitly show the connection between the protein folding problem and spin glass transition. Thi...
The similarity between spin glasses and proteins is that both have complex energy landscapes with mu...
AbstractThe magnetic field dependence of the proton-spin-lattice relaxation rate in rotationally imm...
The way in which the three-dimensional structure of a protein is determined by the one dimensional s...
It is well known among molecular biologists that proteins with a common ancestor and that perform th...
The phase behaviour of small globular proteins is often modeled by approximating them as spherical p...
Intrinsically disordered proteins (IDPs) are proteins that possess large unstructured regions. Their...
Proteins are tiny models of biological complexity: specific interactions among their many amino acid...
URL: http://www-spht.cea.fr/articles/T93/023 (sur invitation). AbstractInternational audienceProtein...
© 2019 American Physical Society.Protein is matter of dual nature. As a physical object, a protein m...
Librational motions in the region of the protein "glass" (or dynamic) transition are analysed for sp...
Folded proteins and spin glasses share various properties, such as seemingly random interactions bet...
Statistical thermodynamics of protein solutions is often studied in terms of simple, microscopic mod...
Proteins are the common constituents of all living cells. They are molecular machines that interact ...
Protein functions require conformational motions. We show here that the dominant conformational moti...
We explicitly show the connection between the protein folding problem and spin glass transition. Thi...
The similarity between spin glasses and proteins is that both have complex energy landscapes with mu...
AbstractThe magnetic field dependence of the proton-spin-lattice relaxation rate in rotationally imm...
The way in which the three-dimensional structure of a protein is determined by the one dimensional s...
It is well known among molecular biologists that proteins with a common ancestor and that perform th...
The phase behaviour of small globular proteins is often modeled by approximating them as spherical p...
Intrinsically disordered proteins (IDPs) are proteins that possess large unstructured regions. Their...
Proteins are tiny models of biological complexity: specific interactions among their many amino acid...
URL: http://www-spht.cea.fr/articles/T93/023 (sur invitation). AbstractInternational audienceProtein...
© 2019 American Physical Society.Protein is matter of dual nature. As a physical object, a protein m...
Librational motions in the region of the protein "glass" (or dynamic) transition are analysed for sp...
Folded proteins and spin glasses share various properties, such as seemingly random interactions bet...
Statistical thermodynamics of protein solutions is often studied in terms of simple, microscopic mod...
Proteins are the common constituents of all living cells. They are molecular machines that interact ...
Protein functions require conformational motions. We show here that the dominant conformational moti...