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    Probing antibody internal dynamics with fluorescence anisotropy and molecular dynamics simulations

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    Name:
    Probing antibody internal dynamics ...
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    Genre
    Journal Article
    Date
    2013-03-01
    Author
    Kortkhonjia, E
    Brandman, R
    Zhou, JZ
    Voelz, VA
    Chorny, I
    Kabakoff, B
    Patapoff, TW
    Dill, KA
    Swartz, TE
    Subject
    monoclonal antibodies
    solution dynamics
    molecular dynamics simulations
    fluorescence anisotropy
    therapeutic antibodies
    Permanent link to this record
    http://hdl.handle.net/20.500.12613/5587
    
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    DOI
    10.4161/mabs.23651
    Abstract
    The solution dynamics of antibodies are critical to antibody function. We explore the internal solution dynamics of antibody molecules through the combination of time-resolved fluorescence anisotropy experiments on IgG1 with more than two microseconds of all-atom molecular dynamics (MD) simulations in explicit water, an order of magnitude more than in previous simulations. We analyze the correlated motions with a mutual information entropy quantity, and examine state transition rates in a Markov-state model, to give coarse-grained descriptors of the motions. Our MD simulations show that while there are many strongly correlated motions, antibodies are highly flexible, with Fab and Fc domains constantly forming and breaking contacts, both polar and non-polar. We find that salt bridges break and reform, and not always with the same partners. While the MD simulations in explicit water give the right time scales for the motions, the simulated motions are about 3-fold faster than the experiments. Overall, the picture that emerges is that antibodies do not simply fluctuate around a single state of atomic contacts. Rather, in these large molecules, different atoms come in contact during different motions. © 2013 Landes Bioscience.
    Citation to related work
    Informa UK Limited
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    mAbs
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    ae974a485f413a2113503eed53cd6c53
    http://dx.doi.org/10.34944/dspace/5569
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