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The Mission of MBR is to provide access to state-of-the-art biophysical instrumentation, experimental design, and analyses to the UTSW community. MBR seeks to accomplish this goal by maintaining a wide variety of such instrumentation and training users regarding its proper operation. Further, users are trained on the analysis and interpretation of their data, if appropriate.

Another means of achieving MBR's aims is for its personnel to enter into collaborative arrangements with principal investigators. These collaborations can take on many forms. For example, MBR personnel can aid in the design and performance of the experiments, or both of these aspects can be handled solely by MBR. Seeking off-campus and industrial collaborations will be an important step in optimally utilizing MBR's considerable resources.

Another important goal of MBR is to develop new and innovative ways to analyze biophysical data. To this end, MBR personnel have authored software for the presentation and analysis of biophyscial data. We plan to continue this effort to extend the current capabilities of biophysiscal analysis.


To ensure the smooth operation and continuous availability of MBR's resources, the following policies have been put in place.

1. All users must be trained by MBR personnel prior to using the equipment.

2. A calendar is maintained by MBR personnel for each instrument. Users must reserve time on an instrument prior to usage. Reservations are made using the iLab system.

3. Users must accurately log their usage.

4. If cancellations are necessary, users are asked to make them as soon as possible, and no later than one hour before the scheduled use. Failure to cancel will result in charges equal to those for the full duration of the resesrvation.

5. Users will be billed for their training and instrument time on a monthly basis.

6. Users and their PIs are responsible for damage to instrumentation that occurs due to negligence.

7. Users will report problems with the operation of an MBR resource promptly to the Director.

8. Each resource has an associated computer. Users will do their best to make sure that any media used in conjunction with these computers is free of malware.

9. Tampering with MBR hardware, software, or computers is strictly forbidden.


Chad Brautigam




Wands, A.M., Cervin, J., Huang, H., Zhang, Y., Youn, G., Brautigam, C.A., Matson, Dzebo M., Björklund, P., Wallenius, V., Bright, D.K., Bennett, C.S., Wittung-Stafshede, P., Sampson, N.S., Yrlid, U., Kohler, J.J. (2018). Fucosylated molecules competitively interfere with cholera toxin binding to host cells.ACS Infect. Dis., 4, 758-770. [PubMed]

Tso, S.-C., Chen, Q., Vishnivetskiy, S.A., Gurevich, V.V., Iverson, T.M. & Brautigam, C.A. (2018). Using two-site models to analyze microscale thermophoresis data. Anal. Biochem., 540-541, 64-75. [PubMed]


Brautigam, C.A., Deka, R.K., Liu, W.Z., & Norgard, M.V. (2016). The Tp0684 (MglB-2) lipoprotein of Treponema pallidum: a glucose-binding protein with divergent topology. PLoS One, 11, e0161022. [PubMed]

Scheuermann, T.H., Padrick, S.B., Gardner, K.H., & Brautigam, C.A. (2016). On the acquisition and analysis of microscale thermophoresis data. Anal. Biochem., 496, 79-93. [PubMed]


Brautigam, C.A. (2015). Fitting two- and three-site binding models to isothermal titration calorimetric data. Methods, 76, 124-136. [PubMed]

Scheuermann, T.H. & Brautigam, C.A. (2015). High-precision, automated integration of multiple isothermal titration calorimetric thermograms: new features of NITPIC. Methods, 76, 87-98. [PubMed]


Ayaz, P., Munyoki, S., Geyer, E.A., Piedra, F.A., Vu, E.S., Bromber, R., Otwinowski, Z., Grishin, N.V., Brautigam, C.A., & Rice, L.M. (2014). A tethered delivery mechanism explains the catalytic action of a microtubule polymerase. eLife, 3, e03069. [PubMed]

Ghirlando, R., Zhao, H., Balbo, A., Piszczek, G., Curth, U., Brautigam, C.A., & Schuck, P. (2014). Measurement of the temperature of the resting rotor in analytical ultracentrifugation. Anal. Biochem., 458, 37-39. [PubMed]

Ouyang, Z., Zhou, J., Brautigam, C.A., Deka, R., & Norgard, M.V. (2014). Identification of a core sequence for the binding of BosR to the rpoS promoter region in Borrelia burgdorferi. Microbiology, 160, 851-862. [PubMed]

Zhang, X., Wu, J., Du, F., Xu, H., Sun, L., Chen, Z., Brautigam, C.A., Zhang, X., & Chen, Z.J. (2014). The cytosolic DNA sensor cGAS forms an oligomeric complex with DNA and undergoes switch-like conformational changes in the activation loop. Cell Rep., 6, 421-430. [PubMed]


Ni, L., Li, S., Yu, J., Min, J., Brautigam, C.A., Tomchick, D.R., Pan, D., & Luo, X. (2013). Structural basis for autoactivation of human Mst2 kinase and its regulation by RASSF5. Structure, 21, 1757-1768. [PubMed]

Wang, Y., Pascoe, H.G., Brautigam, C.A., He, H., & Zhang, X. (2013). Structural basis for activation and non-canonical catalysis of the Rap GTPase activating protein domain of plexin. eLife, 2, e01279. [PubMed]

Ghirlando, R., Balbo, A., Piszczek, G., Brown, P.H., Lewis, M.S., Brautigam, C.A., Schuck, P., & Zhao, H. (2013). Improving the thermal, radial, and temporal accuracy of the analytical ultracentrifuge through external references. Anal. Biochem., 440, 81-95. [PubMed]

Brautigam, C.A., Padrick, S.B., & Schuck, P. (2013). Multi-signal sedimentation velocity analysis with mass conservation for determining the stoichiometry of protein complexes. PLoS One, 8, e62694. [PubMed]

Zhou, H., Ghirlando, R., Piszczek, G., Curth, U., Brautigam, C.A. & Schuck, P. (2013). Recorded scan times can limit the accuracy of sedimentation coefficients in analytical ultracentrifugation. Anal. Biochem., 437, 104-108. [PubMed]


Keller, S., Vargas, C., Zhao, H., Piszczek, G., Brautigam, C.A., Schuck, P. (2012). High-precision isothermal titration calorimetry with automated peak-shape analysis. Anal. Chem., 84, 5066-5073. [PubMed]

Ayaz, P., Ye, X., Huddleston, P., Brautigam, C.A., Rice, L.M. (2012). A TOG:αβ-tubulin complex structure reveals conformation-based mechanisms for a microtubule polymerase. Science, 337, 857-860. [PubMed]


Padrick, S.B. & Brautigam, C.A. (2011). Evaluating the stoichiometry of macromolecular complexes using multisignal sedimentation velocity. Methods, 54, 39-55. [PubMed]

Brautigam, C.A. (2011). Using Lamm-Equation modeling of sedimentation velocity data to determine the kinetic and thermodynamic properties of macromolecular interactions. Methods, 54, 4-15. [PubMed]

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  updated June 6, 2018  
  Department of Biophysics