Molecular dynamics simulations of helix and turn propensities in model peptides
Helices, β-structures, turns and hydrophobic cores are key substructures of proteins, conferring stability on the native conformation, and functioning as early intermediates in the folding process. Molecular dynamics calculations, both as free dynamics simulations and as free energy calculations, ar...
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1993 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: Current Opinion in Structural Biology - Amsterdam : Elsevier, 3(1993), 2, Seite 270-276 |
| Übergeordnetes Werk: |
volume:3 ; year:1993 ; number:2 ; pages:270-276 |
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(DE-627)NLEJ177006854 (DE-599)GBVNLZ177006854 DE-627 ger DE-627 rakwb eng Molecular dynamics simulations of helix and turn propensities in model peptides 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Helices, β-structures, turns and hydrophobic cores are key substructures of proteins, conferring stability on the native conformation, and functioning as early intermediates in the folding process. Molecular dynamics calculations, both as free dynamics simulations and as free energy calculations, are being used to uncover details of the equilibria and kinetics of formation and inter-conversion of these structures in model oligopeptides. This theoretical development parallels experimental studies with synthetic oligopeptides elsewhere. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hermans, J. oth in Current Opinion in Structural Biology Amsterdam : Elsevier 3(1993), 2, Seite 270-276 (DE-627)NLEJ177006358 (DE-600)2019233-2 0959-440X nnns volume:3 year:1993 number:2 pages:270-276 http://dx.doi.org/10.1016/S0959-440X(05)80163-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 3 1993 2 270-276 |
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molecular dynamics simulations of helix and turn propensities in model peptides |
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Molecular dynamics simulations of helix and turn propensities in model peptides |
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Helices, β-structures, turns and hydrophobic cores are key substructures of proteins, conferring stability on the native conformation, and functioning as early intermediates in the folding process. Molecular dynamics calculations, both as free dynamics simulations and as free energy calculations, are being used to uncover details of the equilibria and kinetics of formation and inter-conversion of these structures in model oligopeptides. This theoretical development parallels experimental studies with synthetic oligopeptides elsewhere. |
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Helices, β-structures, turns and hydrophobic cores are key substructures of proteins, conferring stability on the native conformation, and functioning as early intermediates in the folding process. Molecular dynamics calculations, both as free dynamics simulations and as free energy calculations, are being used to uncover details of the equilibria and kinetics of formation and inter-conversion of these structures in model oligopeptides. This theoretical development parallels experimental studies with synthetic oligopeptides elsewhere. |
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Helices, β-structures, turns and hydrophobic cores are key substructures of proteins, conferring stability on the native conformation, and functioning as early intermediates in the folding process. Molecular dynamics calculations, both as free dynamics simulations and as free energy calculations, are being used to uncover details of the equilibria and kinetics of formation and inter-conversion of these structures in model oligopeptides. This theoretical development parallels experimental studies with synthetic oligopeptides elsewhere. |
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