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<?xml version="1.0"?>
<api>
  <query-continue>
    <allpages gapcontinue="Sample_Preparation" />
  </query-continue>
  <query>
    <pages>
      <page pageid="3" ns="0" title="Research">
        <revisions>
          <rev xml:space="preserve">The overall focus of our research has been on the biological interactions which are central to the control of biological function; attempting to relate protein structure, kinetics, dynamics, and thermodynamics to function.
&lt;BR&gt;&lt;BR&gt;
Heart disease is the leading cause of death in western society for men and women. The long term focus of our program is the elucidation of the molecular details of the calcium mediated thin filament based regulation of contraction in cardiac and skeletal muscle. Recent discoveries have seen a great expansion in the number of sacromere proteins, concomitant appreciation of the interconnected cytoskeletal network critical for contractile activity, and a recognition of a large number of mutations in these cytoskeletal components which account for a number of human myopathies. Of special medical importance because of the prevalence of cardiovascular disease are the cardiac regulatory proteins, where phosphorylation of cardiac troponin plays a major role in mediating myofilament physiology; troponin mutations are implicated in various cardiac diseases including familial hypertrophic cardiomyopathy which are amongst the most frequently occurring inherited cardiac disorders; troponin proteins are important markers of cardiovascular damage; and cardiac troponin is subject to influence by cardiotonic drugs, which may be used to modulate the calcium response of the myofilaments in diseased hearts. Thus, there is a strong interest and need in understanding the structure and dynamics of these proteins.
&lt;BR&gt;&lt;BR&gt;
Most of our research involves the determination of the solution structure and dynamics of muscle proteins using high field, multinuclear, multidimension Nuclear Magnetic Resonance spectroscopic techiques. For a recent review of some of our work see: Li MX, Wang X, Sykes BD., J Muscle Res Cell Motil. 2004;25(7):559-79. Structural based insights into the role of troponin in cardiac muscle pathophysiology.
&lt;BR&gt;&lt;BR&gt;
We are also developing new solid state NMR techniques for the determination of the orientation and in situ structures of the thin filament regulatory proteins in intact muscle fibers. This will allow us to connect high resolution structural and dynamic changes to physiological and functional measurements (i.e., force).</rev>
        </revisions>
      </page>
      <page pageid="40" ns="0" title="Running NMR spectrum">
        <revisions>
          <rev xml:space="preserve">Typical parameters for nmr600:

Spectra were acquired on a 600-MHz Inova NMR spectrometer at 25 °C using the tn noesy pulse sequence (circa Vnmr 6.1B software, Varian Inc). 

Spectra had an acquisition time of 4 s, a preacquisition delay of 1 s, a mixing time of 0.1 s, a sweep width of 7200 Hz, and 256 transients.

 {Saude, E. J., Slupsky, C. M., and Sykes, B. D. (2006) Metabolomics 2, 113-123}

   ACQUISITION            SAMPLE            PROCESSING        2D PROCESSING
 sfrq       599.856  date   Sep 29 2010  lb        not used  lb1       not used
 tn              H1  solvent        D2O  sb        not used  sb1         -0.085
 at           4.000  temp          30.0  gf        not used  sbs1        -0.085
 np           67184      DECOUPLING      proc            ft  gf1       not used
 sw          8398.1  dn                  fn          262144  fn1           2048
 bs               8  dof        -3326.9  ssfilter  not used        FLAGS
 ss               2  dm            nnnn  ssorder   not used  dp               y
 tpwr            58  dmm           cccp  ssntaps        200  C13refoc         n
 pw             8.8  dpwr            48  sslsfrq   not used  N15refoc         n
 d1           0.010  homo             n      GRADIENTS       CNrefoc          n
 d2               0    2D ACQUISITION    gt1         0.0030      SATURATION
 mix          0.100  sw1         8398.1  gzlvl1        5000  mfsat            n
 tof         -219.5  ni               1  gt2         0.0050  sspul            n
 nt             256  phase            1  gzlvl2        7500  satmode       ynyn
 ct             256                                          satpwr           6
                                                             satdly       0.990
                                                             scuba            n</rev>
        </revisions>
      </page>
    </pages>
  </query>
</api>