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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Il nuovo cimento della Società Italiana di Fisica 17 (1995), S. 983-991 
    ISSN: 0392-6737
    Keywords: General, theoretical, and mathematical biophysics (including logic of biosystems, quantum biology, and relevant aspects of thermodynamics, information theory, cybernetics, and bionics) ; Molecular dynamics, conformational changes, and pattern recognition in biomolecules ; Physical chemistry of solutions of biological macromolecules
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Summary We introduce a general scheme to assign statistical weights to alla priori pathways in conformation space for an aggregate of interacting particles that undergoes a series of unimolecular events in a limited time frame. Illustrations of such systems are biopolymers that fold intramolecularly or macromolecules of biological relevance that exert their function onto themselves through a series of structural rearrangements under the severe time constraints imposed by enzymatic timing. We endow the space of kinetically controlled pathways with a regular measure induced by a stochastic process built upon a complex potential energy landscape. This process simulates the progressive and opportunistic exploration of basins of attraction of critical points in the molecular potential energy. The derivation is general and holds for any diffusion-like process subject to time constraints and governed by thermal fluctuations upon a complex energy landscape. Within this framework, the ensemble of physically relevant kinetically arrested states becomes a cross-section of the ensemble of pathways at a fixed instant.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 23 (1995), S. 218-232 
    ISSN: 0887-3585
    Keywords: protein conformation ; protein stability ; sensitivity analysis ; avian pancreatic polypeptide (APP) ; molecular dynamics simulation ; OPLS/Amber force field ; continuum solvation model ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Computer simulations utilizing a classical force field have been widely used to study biomolecular properties. It is important to identify the key force field parameters or structural groups controlling the molecular properties. In the present paper the sensitivity analysis method is applied to study how various partial charges and solvation parameters affect the equilibrium structure and free energy of avian pancreatic polypeptide (APP). The general shape of APP is characterized by its three principal moments of inertia. A molecular dynamics simulation of APP was carried out with the OPLS/Amber force field and a continuum model of solvation energy. The analysis pinpoints the parameters which have the largest (or smallest) impact on the protein equilibrium structure (i.e., the moments of inertia) or free energy. A display of the protein with its atoms colored according to their sensitivities illustrates the patterns of the interactions responsible for the protein stability. The results suggest that the electrostatic interactions play a more dominant role in protein stability than the part of the solvation effect modeled by the atomic solvation parameters. © 1995 Wiley-Liss, Inc.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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