Explore UAB

Faculty active in this area of research are listed below. For a brief description of their research interests, click on their name in the list. Clicking on the name at the beginning of the brief description links to their detailed personal website.



J. Edwin Blalock, PhD, Department of Medicine
Mark R. Walter, PhD, Department of Microbiology



J. Edwin Blalock, PhD  The overall objective of our current research is to delineate certain genetic rules that govern the shape and function of proteins and peptides. Specifically, nucleic acids encode amino acid sequences in a binary fashion with regard to hydropathy. We and others have provided compelling evidence that the exact pattern of polar and nonpolar amino acids, rather than the precise identity of particular R groups, is an important driving for protein shape. Structural proof for this idea is being pursued through determination of the 3-dimensional structures of peptides with dissimilar primary amino acid sequences but identical binary codes. These design principles are being used: 1) to make synthetic peptides specifically targeted to act as agonists and antagonists of Ca++ channels involved in human immunodeficiency virus-mediated apoptosis and 2) to make synthetic peptide vaccines as immunotherapeutic agents against autoimmune diseases of the nervous system such as myasthenia gravis (MG) and multiple sclerosis (MS). Additional research areas include: First, together with colleagues at the University of Utrecht, we are evaluating the aforementioned peptide regulators of Ca++ channels for utility in models of asthma. Second, together with Dick Marchase's group, we are elucidating the structure and function of a novel Ca++ influx factor (CIF) which is a key signal for store-operated Ca++ entry. Third, we are studying the role of these CIF-operated channels, as well as their regulation by glucosamine in diabetes.


Mark R. Walter, PhD The Walter lab is interested in protein-protein interactions and structural biology of macromolecular complexes required to elicit effective host immune responses against pathogens. Studies have focused on the IL-10 family (IL-10, IFN-γ, IL-20, IL-22, IL-24, IL-26, IL-28, and IL-29) of cytokine receptor complexes that play essential roles in the development and control of the adaptive immune response. The inter-cellular communication provided by these molecules is controlled by a dazzling array of protein-protein interactions that our lab is unraveling. We also study the structure and function of virally encoded proteins produced by herpesviruses and poxviruses that target the IL-10 family and allow the viruses to escape elimination by the immune system. Understanding the competing molecular strategies used by the host and virus to activate or deactivate the immune system may to lead novel ways of controlling chronic inflammation and/or improving the detection and elimination of persistent viral infections.

The lab performs the techniques required to answer mechanistic questions about molecular recognition, viral immune evasion, and cell signaling including protein biochemistry, X-ray crystallography, Surface Plasmon Resonance, computational and bioinformatic approaches, and structure-based functional assays in cells.