Biography

orban


CONTACT INFORMATION

 Office Phone: 240-314-6221
 Office Address: 0130
 Email: jorban@umd.edu
 Group Website

Professor

Education

  • Ph.D. Chemistry, Australian National University,1985.
  • CSIRO Postdoctoral Fellow, 1985-1987.

Research Interests

My research interests are focused in the area of protein structural biology and design, particularly in understanding how the malleability of protein folds relates to biological function. High field solution NMR spectroscopy and other biophysical and biochemical methods are employed in my laboratory.

Research

My research interests are focused in the area of protein structural biology and design, particularly in understanding how the malleability of protein folds relates to biological function. High field solution NMR spectroscopy and other biophysical and biochemical methods are employed in my laboratory.

A major interest is in the design and biophysical characterization of proteins with high sequence identity but completely different fold topologies (heteromorphic proteins). This study has led to the surprising result that two proteins with different folds can come very close in sequence space – the 3α albumin-binding domain (GA) and the 4β+α IgG-binding domain (GB) of streptococcal protein G can interconvert through a very short mutational pathway. Moreover, this path is not unique and large-scale fold changes can be effected in multiple ways with successive single amino acid mutations at diverse residue positions. Even residue substitutions on the periphery of the protein core can tip the balance between alternatively folded GA and GB states.

 

These studies have relevance to further understanding the relationship between amino acid sequence and three-dimensional structure, and have implications in computational protein structure prediction, fold evolution studies, and human disease. Other related interests include allosteric and large-scale changes in conformation upon ligand binding, and the role of intrinsically disordered regions in protein-protein interactions.

Support from the NIH, NSF, DOE and Keck Foundation is gratefully acknowledged.

Print Friendly