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    Investigations of peptide hydration using NMR and molecular dynamics simulations: A study of effects of water on the conformation and dynamics of antamanide

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    Authors
    Peng, Jeffrey W.
    Schiffer, Celia A.
    Xu, Ping
    van Gunsteren, Wilfred F.
    Ernst, Richard R.
    UMass Chan Affiliations
    Department of Biochemistry and Molecular Pharmacology
    Document Type
    Journal Article
    Publication Date
    1996-12-01
    Keywords
    Peptides, Cyclic
    Water
    Molecular Dynamics Simulation
    Molecular Conformation
    Nuclear Magnetic Resonance, Biomolecular
    Biochemistry, Biophysics, and Structural Biology
    Pharmacology, Toxicology and Environmental Health
    
    Metadata
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    Link to Full Text
    http://dx.doi.org/10.1007/BF00228147
    Abstract
    The influence of water binding on the conformational dynamics of the cyclic decapeptide antamanide dissolved in the model lipophilic environment chloroform is investigated by NMR relaxation measurements. The water-peptide complex has a lifetime of 35 mgrs at 250 K, which is longer than typical lifetimes of water-peptide complexes reported in aqueous solution. In addition, there is a rapid intracomplex mobility that probably involves librational motions of the bound water or water molecules hopping between different binding sites. Water binding restricts the flexibility of antamanide. The experimental findings are compared with GROMOS molecular dynamics simulations of antamanide with up to eight bound water molecules. Within the simulation time of 600 ps, no water molecule leaves the complex. Additionally, the simulations show a reduced flexibility for the complex in comparison with uncomplexed antamanide. Thus, there is a qualitative agreement between the experimental NMR results and the computer simulations.
    Source
    Peng, J.W., Schiffer, C.A., Xu, P., van Gunsteren, W.F., Ernst, R.R. "Dynamics of Antamanide with Water in Chloroform." J. Biol. NMR 8:453-476 (1996).
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/25982
    PubMed ID
    20859779
    Collections
    UMass Chan Faculty and Researcher Publications
    Schiffer Lab Publications

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