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<article data-history-node-id="13571" about="/labs-at-nibib/trans-nih-shared-resource-biomedical-engineering-and-physical-science-beps/quantitative-methods-macromolecular-interactions" class="intramural-research-program node--irp node--type-intramural-research-program">
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<div class="field field--name-body field--type-text-with-summary field--label-hidden field__item"><p>The Quantitative Methods for Macromolecular Interactions (QMMI) Unit of the BEPS Shared Resource has expertise in:</p>
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<ul>
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<li>Characterization of individual macromolecules</li>
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<li>Characterization of interactions of macromolecules (self- and hetero association) and small ligands</li>
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<div class="field field--name-field-lab-resources field--type-text-long field--label-hidden field__item"><p><img alt class="media-element file-default media-float-right" height="120" src="/sites/default/files/AUC3Crop72dpi.png" style="width: 128px; height: 120px; float: right;" title typeof="foaf:Image" width="128"></p>
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<p>QMMI is experienced in the application of a wide array of state-of-the-art biophysical instrumentation toward the characterization of individual macromolecules, as well as their interactions with other macromolecules or small ligands. This characterization may include:</p>
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||
<ul>
|
||
<li>Determination of equilibrium binding constants
|
||
<ul>
|
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<li>thermodynamics (Delta G, Delta H, Delta Cp)</li>
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<li>kinetics (kon, koff)</li>
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</li>
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<p><img alt class="media-element file-default media-float-right" height="119" src="/sites/default/files/MicroC5Crop72dpi.png" style="width: 128px; height: 119px; float: right;" title typeof="foaf:Image" width="128"></p>
|
||
<ul>
|
||
<li>Measurement of solution-phase molecular weight, sedimentation coefficients, and translational diffusion coefficients, hydrodynamic radius, and overall asymmetry of macromolecules or their assemblies</li>
|
||
<li>Establishment of the stoichiometry of complexes</li>
|
||
<li>Insight into secondary structure or changes in structure upon ligand binding</li>
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</ul>
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<p><strong><em>The following analytical techniques are available within the QMMI Unit. <a href="/research/labs-at-nibib/biomedical-engineering-and-physical-science-beps-shared-resource/quantitative/pricing-for-qmmi">Click here for pricing information.</a></em></strong></p>
|
||
<h3>Analytical ultracentrifugation (AUC) SV/SE</h3>
|
||
<ul>
|
||
<li>Brown PH, Balbo A, Schuck P. On the analysis of sedimentation velocity in the study of protein complexes. Eur Biohpys J, 38, (8), 1079-1099, 2009.</li>
|
||
<li>Balbo A, Zhao H, Brown PH, Schuck P. Assembly, loading, and alignment of an analytical ultracentrifuge sample cell. J Vis Exp, 33, pii 1530, 2009.</li>
|
||
<li>Brown PH, Balbo A, and Schuck P. Characterizing protein-protein interactions by sedimentation velocity analytical ultracentrifugation. Current Protocols in Immunology, Chapter 18: Unit 18.15, 2008.</li>
|
||
<li>Balbo A, Brown PH, Braswell EH, and Schuck P. Measuring protein-protein interactions by equilibrium sedimentation. Current Protocols in Immunology, Chapter 18: Unit 18.8, 2007.</li>
|
||
<li>Lebowitz J, Lewis MS, Schuck P. Protein Science, 11:2067-2079, 2002.</li>
|
||
</ul>
|
||
<h3>Isothermal titration calorimetry (ITC)</h3>
|
||
<ul>
|
||
<li>Jelesarov I and Bosshard HR. Journal of Molecular Recognition, 12:3-18, 1999.</li>
|
||
<li>Pierce MM, Raman CS, Nall BT. Methods, 19:213-221, 1999.</li>
|
||
<li>Velazquez-Campoy A, Leavitt, SA, Freire E. Methods in Molecular Biology, 261:35 -54, 2004.</li>
|
||
</ul>
|
||
<h3>Dynamic light scattering (DLS)</h3>
|
||
<ul>
|
||
<li>Wyatt, PJ. Analytica Chimica Acta, 272:1-40, 1993. Surface Plasmon Resonance (SPR)</li>
|
||
</ul>
|
||
<h3>Surface Plasmon Resonance (SPR)</h3>
|
||
<ul>
|
||
<li>Schuck P. Annu. Rev. Biophys. Biomol. Struct. 26: 541-566, 1997. <em>For more information, see the</em> <a href="/labs-at-nibib/trans-nih-shared-resource-biomedical-engineering-and-physical-science-beps/micro">Micro Analytical Immunochemistry SPR</a><em> page.</em></li>
|
||
</ul>
|
||
<h3>Differential scanning calorimetry (DSC)</h3>
|
||
<ul>
|
||
<li>Cooper AM, Nutley, A and Wadwood A. Differential scanning microcalorimetry. In Protein-ligand Interactions: hydrodynamics and calorimetry, pp. 287-318. Edited by S. E. Harding & B. Z. Chowdry, New York: Oxford University Press, 2000.</li>
|
||
<li>Jelesarov I and Bosshard HR. Journal of Molecular Recognition, 12, 3-18, 1999.</li>
|
||
</ul>
|
||
<h3>Circular dichroism spectroscopy (CDS</h3>
|
||
<ul>
|
||
<li>Kelly S and Price N. Current Protocols in Protein Science, 20.10.1 – 20.10.18, 2006.</li>
|
||
<li>Kelly S, Ness, TJ, and Price, N. Biochimica et Biophysica Acta, 1751:119-139, 2005.</li>
|
||
<li>Provencher SW and Glöckner J Biochemistry, 20:33-37, 1981</li>
|
||
</ul>
|
||
<h3>Asymmetric flow field-flow fractionation (AF4)</h3>
|
||
<ul>
|
||
<li>Ratanathanawongs SK and Williams DL. J Sep Sci, 29:1720 – 1732, 2006.</li>
|
||
<li>Fraunhofer W and Winter G. European Journal of Pharmaceutics and Biopharmaceutics, 58: 369-383, 2004.</li>
|
||
<li>Fraunhofer W, Winter G, and Coester C. Anal Chem, 76:1909-1920, 2004.</li>
|
||
</ul>
|
||
<h3>Spectrofluorometry</h3>
|
||
<ul>
|
||
<li>Lee, C. Y. 2009. Fluorescence Spectroscopy. Current Protocols Essential Laboratory Techniques. 2:2.4.1–2.4.29. DOI: 10.1002/9780470089941.et0204s02</li>
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<div class="field field--name-field-pubmed field--type-string-long field--label-hidden field__item"><div class='nav nav-tabs pub-date-tabs'><button data-toggle="tab" href="#tab-2012">2012</button><button data-toggle="tab" href="#tab-2010">2010</button><button data-toggle="tab" href="#tab-2009">2009</button><button data-toggle="tab" href="#tab-2007">2007</button></div><div class="tab-content pub-tab-content"><div id="tab-2012" class="tab-pane"><div class="publication"><div class="title"><a href="https://www.ncbi.nlm.nih.gov/pubmed/22508847&api_key=6850ce796fb3324610d4762dca788159ad08" title="Go to PubMed Article">Analysis of high-affinity assembly for AMPA receptor amino-terminal domains.</a></div><div class="authors"><span>Zhao H</span><span>Berger AJ</span><span>Brown PH</span><span>Kumar J</span><span>Balbo A</span><span>May CA</span><span>Casillas E</span><span>Laue TM</span><span>Patterson GH</span><span>Mayer ML</span><span>Schuck P</span></div><div class="iso">J Gen Physiol</div><div class="date">2012 May</div></div><br />
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</div><div id="tab-2010" class="tab-pane"><div class="publication"><div class="title"><a href="https://www.ncbi.nlm.nih.gov/pubmed/20480511&api_key=6850ce796fb3324610d4762dca788159ad08" title="Go to PubMed Article">Accounting for solvent signal offsets in the analysis of interferometric sedimentation velocity data.</a></div><div class="authors"><span>Zhao H</span><span>Brown PH</span><span>Balbo A</span><span>Fernández-Alonso Mdel C</span><span>Polishchuck N</span><span>Chaudhry C</span><span>Mayer ML</span><span>Ghirlando R</span><span>Schuck P</span></div><div class="iso">Macromol Biosci</div><div class="date">2010 Jul 07</div></div><br />
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<div class="publication"><div class="title"><a href="https://www.ncbi.nlm.nih.gov/pubmed/20166740&api_key=6850ce796fb3324610d4762dca788159ad08" title="Go to PubMed Article">Direct interaction of the mouse cytomegalovirus m152/gp40 immunoevasin with RAE-1 isoforms.</a></div><div class="authors"><span>Zhi L</span><span>Mans J</span><span>Paskow MJ</span><span>Brown PH</span><span>Schuck P</span><span>Jonjić S</span><span>Natarajan K</span><span>Margulies DH</span></div><div class="iso">Biochemistry</div><div class="date">2010 Mar 23</div></div><br />
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</div><div id="tab-2009" class="tab-pane"><div class="publication"><div class="title"><a href="https://www.ncbi.nlm.nih.gov/pubmed/19017632&api_key=6850ce796fb3324610d4762dca788159ad08" title="Go to PubMed Article">Autoinhibition of Arf GTPase-activating protein activity by the BAR domain in ASAP1.</a></div><div class="authors"><span>Jian X</span><span>Brown P</span><span>Schuck P</span><span>Gruschus JM</span><span>Balbo A</span><span>Hinshaw JE</span><span>Randazzo PA</span></div><div class="iso">J Biol Chem</div><div class="date">2009 Jan 16</div></div><br />
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</div><div id="tab-2007" class="tab-pane"><div class="publication"><div class="title"><a href="https://www.ncbi.nlm.nih.gov/pubmed/18027911&api_key=6850ce796fb3324610d4762dca788159ad08" title="Go to PubMed Article">Two interferons alpha influence each other during their interaction with the extracellular domain of human type interferon receptor subunit 2.</a></div><div class="authors"><span>Schmeisser H</span><span>Gorshkova I</span><span>Brown PH</span><span>Kontsek P</span><span>Schuck P</span><span>Zoon KC</span></div><div class="iso">Biochemistry</div><div class="date">2007 Dec 18</div></div><br />
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<div class="publication"><div class="title"><a href="https://www.ncbi.nlm.nih.gov/pubmed/17192587&api_key=6850ce796fb3324610d4762dca788159ad08" title="Go to PubMed Article">Studying multisite binary and ternary protein interactions by global analysis of isothermal titration calorimetry data in SEDPHAT: application to adaptor protein complexes in cell signaling.</a></div><div class="authors"><span>Houtman JC</span><span>Brown PH</span><span>Bowden B</span><span>Yamaguchi H</span><span>Appella E</span><span>Samelson LE</span><span>Schuck P</span></div><div class="iso">Protein Sci</div><div class="date">2007 Jan</div></div><br />
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