dorsal/arxiv
View SchemaThermodynamic Sampling of Molecular Conformations
| Authors | Andreas Kraemer |
|---|---|
| Categories | |
| ArXiv ID | physics/0401036 |
| URL | https://arxiv.org/abs/physics/0401036 |
Abstract
Torsional-space Monte Carlo simulations of flexible molecules are usually based on the assumption that all values of dihedral angles have equal probability in the absence of atomic interactions. In the present paper it is shown that this assumption is not valid. Thermodynamic sampling using dihedral angles or other internal coordinates has to account for both the correct metric in conformational space and the conformation-dependence of the moment of inertia tensor. Metric and moment of inertia terms appear as conformation-dependent factors in the partition function and are obtained by proper separation of internal and rotational degrees of freedom. The importance of both factors is discussed for a number of short peptides as well as for the folded and unfolded states of a protein. It is concluded that thermodynamic Monte Carlo simulations of protein folding that neglect these correction factors tend to underestimate the stability of the folded state.
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"abstract": "Torsional-space Monte Carlo simulations of flexible molecules are usually\nbased on the assumption that all values of dihedral angles have equal\nprobability in the absence of atomic interactions. In the present paper it is\nshown that this assumption is not valid. Thermodynamic sampling using dihedral\nangles or other internal coordinates has to account for both the correct metric\nin conformational space and the conformation-dependence of the moment of\ninertia tensor. Metric and moment of inertia terms appear as\nconformation-dependent factors in the partition function and are obtained by\nproper separation of internal and rotational degrees of freedom. The importance\nof both factors is discussed for a number of short peptides as well as for the\nfolded and unfolded states of a protein. It is concluded that thermodynamic\nMonte Carlo simulations of protein folding that neglect these correction\nfactors tend to underestimate the stability of the folded state.",
"arxiv_id": "physics/0401036",
"authors": [
"Andreas Kraemer"
],
"categories": [
"physics.chem-ph",
"cond-mat.stat-mech"
],
"title": "Thermodynamic Sampling of Molecular Conformations",
"url": "https://arxiv.org/abs/physics/0401036"
},
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