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The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
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Many common substances around us exist as a solution, such as ocean water, air, and gasoline. All solutions are mixtures of substances that are composed of varying amounts of two or more types of atoms or molecules. A mixture with a non-uniform composition is a heterogeneous mixture, whereas a mixture with a uniform composition is a homogeneous mixture. The components that make the homogeneous mixture are evenly spread out and thoroughly mixed. 
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Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules
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Obscurin is a semi-flexible molecule in solution.

Jacob A Whitley1, Aidan M Ex-Willey1,2, Daniel R Marzolf1

  • 1Department of Chemistry and Biochemistry, James Madison University, Harrisonburg, Virginia, 22807.

Protein Science : a Publication of the Protein Society
|January 23, 2019
PubMed
Summary

Giant protein obscurin, composed of immunoglobulin-like (Ig-like) domains, remains extended yet flexible. Its structure allows it to link cellular targets over large distances, acting like a spring for greater extensions.

Keywords:
MDNMRSAXSdomain/domain interactionobscurinstretch

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Obscurin is a large, modular cytoskeletal protein primarily composed of tandem immunoglobulin-like (Ig-like) domains.
  • Short linkers (3-4 residues) connect these Ig-like domains, influencing the protein's overall structure and dynamics.
  • The physical implications of these short linkers on obscurin's flexibility and function remain largely unknown.

Purpose of the Study:

  • To investigate the structural and dynamic properties of tandem obscurin Ig-like domains.
  • To elucidate how short linkers impact the flexibility and physical behavior of obscurin.
  • To understand the implications of obscurin's flexibility for its role in connecting cellular targets.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy
  • Small-angle X-ray scattering (SAXS)
  • Molecular Dynamics (MD) simulations

Main Results:

  • Tandem obscurin Ig-like domains maintain a relatively extended conformation in solution due to interactions at domain poles.
  • Experimental and computational methods reveal significant bending and flexing capabilities in these extended domains.
  • A simplified model demonstrates obscurin's capacity to bridge targets over 200 nm, with increasing energetic cost for further elongation.

Conclusions:

  • Obscurin's modular Ig-like domain structure facilitates long-range target linkage within the cell.
  • Despite an extended stance, obscurin exhibits substantial flexibility, enabling dynamic interactions.
  • The protein functions akin to a spring, allowing for significant extension but requiring more energy for greater distances.