Research Overview Structural Biology
Structural biology is a branch of molecular biology concerned with the study of the architecture and shape of large biological molecules (macromolecules)----including proteins and nucleic acids (DNA and RNA) in particular. Structural biology examines the physical and chemical basis for the complex structures adopted these molecules. This subject is of great interest to biologists, because macromolecules carry out most of the functions of living cells. Typically, these functions depend on proteins, DNA and RNA adopting a specific three-dimensional shape. These shapes depend, in ways that can be predicted and measured, on the basic chemical structure of the molecules-specifically, on the amino acid sequence of proteins and on the nucleotide sequence of DNA or RNA... Complete Information... | Research DescriptionResearch Area: Structural Biology
Research Specialties: NMR Spectroscopy in Structural and Functional Genomics, Protein Folding and Stability, Multidomain Proteins My research interests are focused on the application of high field NMR spectroscopic methods to determine novel protein structures in order to gain insight into function at the molecular level. Related to this area, I am also interested in probing the complex relationship between protein sequence and structure. While NMR spectroscopy plays a key role in most of our studies, my laboratory also uses a number of other biophysical tools as well as bioinformatics, chemistry, biochemistry, and molecular biology techniques. Two main projects currently underway in the lab are summarized briefly here. I. The Protein Folding Code - Conformational Switching and the Evolution of New Folds
How does the amino acid sequence of a protein determine its three-dimensional structure? Understanding the relation between protein sequence and structure is a significant issue in structural genomics and deciphering the protein foldingfolding code remains one of the fundamental unsolved problems in structural biology. We have been using small IgG- and albumin-binding domains from Streptococcal Protein G as model systems to study conformational switching between alpha and beta structures with a range of genetic and biophysical tools. A key question we are investigating... Complete Information... |
Representative PublicationsAlexander, P. A., He, Y., Chen, Y., Orban, J., and Bryan, P. N. (2007) The design and characterization of two proteins with 88% sequence identity but different structure and function. Proc. Natl. Acad. Sci. USA 104, 11963-11968.
He, Y., Chen, Y., Rozak, D. A., Bryan, P. N., and Orban, J. (2007) An Artificially Evolved Albumin Binding Module Facilitates Chemical Shift Epitope Mapping of GA Domain Interactions with Phylogenetically Diverse Albumins. Protein Sci. 16, 1490-1494.
Sari, N., He, Y., Doseeva, V., Surabian, K., Ramprakash, J., Schwarz, F., Herzberg, O., and Orban, J. (2007) Solution Structure of HI1506, a Novel Two-Domain Protein from Haemophilus influenzae. Protein Sci. 16, 977-982.
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