A wide variety of solution biophysics and thermodynamics tools are utilized by SCSB faculty. 
Our faculty include many prominent researchers in these fields. Solution biophysics and thermodynamics techniques are used both as a primary research tool and to guide structural studies.
For example:
Analytical ultra centrifugation studies of cytochrome p450 orthologues led to the successful crystallization and structure solution of the first open-form of a p450 (1).
The use of osmolytes to stabilize partially structured regions of proteins was pioneered at UTMB (2). These techniques have been widely adopted in the structural biology community in the study of protein structure.
Mass spectrometry is now used both as a routine analytical assay of protein sequence and also as a probe of structure (3). Mass spectrometry is the final test of protein sequence, and homogeneity after expression and purification. However, examination of the proteolytic products of a protein can reveal many things. A simple limited proteolysis may reveal domains or disordered regions. Attachment of specific proteolytic agents to a protein can reveal which elements are in proximity, and thereby provide specific structural information in the absence of NMR or crystal data.
SCSBMB Solution Biophysics Core instrumentation - All instrumentation is housed on the fifth floor of the Medical Research Building. Major items include:
- MALDI Mass Spectrometer - routinely used to check purity of protein and peptide samples.
- Beckman Analytical Ultracentrifuge - useful in evaluating protein-protein interaction thermodynamics.
- FTIR - provides a means of evaluating secondary structure of proteins forced to fold by osmolytes.
- Dynamic Light Scattering Apparatus - DLS evaluates the hydrodynamic radius of macromolecules and macromolecular complexes. Intrinsically disordered proteins and their contraction and folding can be monitored using this technique.
- ThermoFluor high throughput screening assay instrumentation (1). This multipurpose high-throughput instrument can be used in an isothermal or thermal scan mode. It uses 384 well plates and in the thermal scan mode is designed to detect fluorescence of fluorophores that bind to the thermally denatured states of proteins. Ligands or solution conditions that stabilize the protein increase the melting temperature (2). Thus, the instrument can be used to optimize solution conditions for protein stability, assess binding constants of small ligands or protein binding partners to a particular protein (3). It can also be used for determining appropriate solution conditions for protein crystallization, enzyme assay development, or drug discovery.