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Professor Emeritus Philip L. Yeagle
picture Professor Emeritus Philip L. Yeagle
University of Connecticut
Molecular & Cell Biology
91 North Eagleville Road - Unit 3125
Storrs, CT 06269-3125
Telephone:
Fax: (860) 486-4331
E-Mail: philip.yeagle@uconn.edu
Visit Professor Emeritus Yeagle's Website.

Education: Ph.D. Duke University

Research Interests:

Current research efforts are focused on the unsolved problem of membrane protein structure. We developed a new segmented approach to the structure of membrane proteins and have used it to successfully solve three dimensional structures at medium resolution for bacteriorhodopsin and bovine rhodopsin both in the dark-adapted state and the activated state of rhodopsin. This is the first structure for an activated G-protein coupled receptor. More recently our studies have explored structure and dynamics in lactose permease, a membrane transport protein. Currently we are exploring structure in two integral membrane proteins, E. coli signal peptidase (with D. Kendall from MCB) and bovine peripherin/rds from retinal rod cells.

Selected Publications:

“Peripherin-2:  an intracellular analogy to viral fusion proteins”,  T. Edrington, R. Lapointe, P.L. Yeagle, Cheryl L. Gretzula, and K. Boesze-Battaglia, Biochemistry, 46, 3605-3613 (2007).

Calcium dependent association of calmodulin with the C-terminal domain of the tetraspanin protein peripherin/rds”, T.C. Edrington V, P.L. Yeagle, Cheryl L. Gretzula, and K. Boesze-Battaglia, Biochemistry, 46, 3862-3871 (2007).

 “Transmembrane helices may flex to satisfy hydrophobic mismatch,” Michael Bennett, Vincent Lemaître, Anthony Watts and Philip L. Yeagle, Biochim. Biophys. Acta, 1768, 530-537 (2007).

 “The tetraspanning protein, peripherin-2, complexes with melanoregulin, a putative membrane fusion regulator”, Kathleen Boesze-Battaglia, Lisa Pankoski-Walker, Cheryl Gretzula, Linda Otis, Bridget Gallagher, Rivka A. Rachel, Nancy A. Jenkins, Neal G. Copeland, Francine Morris, Philip Yeagle and Monika Damek-Poprawa, Biochemistry, 46, 1256 - 1272 (2007).

“Differential stability among the transmembrane helices of lactose permease may be important to transport”, Michael Bennett, Robert d'Rozario, Mark Sansom and Philip L. Yeagle, Biochemistry, 45, 8088-8095 (2006).

“Molecular Dynamic Simulations Of Retinal In Rhodopsin: From The Dark-Adapted State Towards Lumirhodopsin,” Vincent Lemaître, Philip L.Yeagle, and Anthony Watts, Biochemistry44, 12667-80 (2005).

“Stability of loops in the structure of lactose permease”, Michael Bennett, James A. Yeagle, Mark Maciejewski, James Ocampo, and P. L. Yeagle, Biochemistry, 43, 12829-12837, (2004).

"A conformational trigger for the activation of a G protein by a G protein coupled receptor", Philip L. Yeagle and Arlene D. Albert, Biochemistry, 42, 1365-1368 (2003).

"Structural studies of Metarhodopsin II, the activated form of the G-protein coupled receptor, rhodopsin", Gregory Choi, Judith Landin, Jhenny Flor Galan, Robert R. Birge, Arlene D. Albert and Philip L. Yeagle, Biochemistry,
41, 7318-7324 (2002).

"Studies on the structure of the G-protein coupled receptor rhodopsin including the putative G-protein binding site in unactivated and activated forms", Philip L. Yeagle, Gregory Choi, and Arlene D. Albert Biochemistry,
40, 11932-11937 (2001).

"Assembly of a polytopic membrane protein structure from the solution structures of overlapping peptide fragments of bacteriorhodopsin", Madan Katragadda, James L. Alderfer and Philip L. Yeagle, Biophys. J.
81: 1029-1036 (2001).

"Three Dimensional Structure of the Seventh Transmembrane Helical Domain of the G-protein Receptor, Rhodopsin", Philip L. Yeagle, Chad Danis, Gregory Choi, James L. Alderfer and Arlene D. Albert, Mol. Vision,
6, 125-131 (2000). Online version is here.