Research of the group of Petra Fromme
at Arizona State University
Biophysical Chemistry of Membrane Proteins
 |
Schematic picture of a Biological Membrane |
Overview
The unraveling of the structure and function of membrane proteins is one of the most challenging goals in the post-genomic era.
The most important processes in all living cells, which include simple living forms such as bacteria and simple eukaryotic cells as well as plants, animals, and humans are catalyzed by membrane proteins. For example, respiration, photosynthesis, cell communication, cell import/export, cell-growth and recognition are catalyzed and regulated by membrane proteins. The proteins do not act on their own, instead they perform communication within the cells by binding and releasing of cofactors and soluble signal-transducing proteins.
 |
Important function of membraneproteins
|
The main step for the elucidation of these complex processes in whole living cells is the understanding of the structure, dynamics and function of the membrane proteins, which play the key role in these processes.
The great importance of membrane proteins as the major key player in the function of all living cells, being targets for more than 50% of all drugs, stands in contrast to the lack of knowledge on their structure and function, the main deficit being the lack of structural information. More than 25 000 structures of soluble proteins have been solved so far by X-ray structure analysis or NMR spectroscopy, whereas only structures of less than 50 functional and structural different membrane proteins have been worldwide solved so far. The crystallization is the rate-limiting step for the elucidation of their structure and function. The deeper understanding of the physical chemical processes, which occur during membrane protein crystallization, is therefore one major research topic of my group.
The X-ray structure of membrane proteins provides detailed structural information on one static functional state of the protein and is therefore the basis for the understanding of their function. It is exciting to extend this picture to the understanding of more complex processes essential to the function of the membrane proteins, e.g., the interaction with signaling molecules, proteins, cofactors, and drugs. Therefore, a further challenge in my work on membrane proteins also lies in the unraveling of the dynamics of membrane proteins.
The main step for the elucidation of these complex processes in whole living cells is the understanding of the whole pictures of the structure, dynamics and function of the membrane proteins as the key players in important cell processes. Spectroscopic spectator labels will be introduced to allow the investigation of these processes in reconstituted protein, the protein detergent micelles and even in the single crystals. These investigations are of a very interdisciplinary nature and include biochemical investigations, molecular biology, spectroscopy, structural investigations by X-ray structure analysis as well as theoretical investigations.
Current Research Projects
|
 |
Interaction of Photosystem I with its natural electron acceptors ferredoxin and cytochrome c6/plastocyanin
Group members working on this project:
HongQi Yu, Raimund Fromme, Yana Bukman and Daqun Ni
cooperation with
R. Blankenship (ASU), P. Setif (CEA, France), D. Matyushov (ASU)
|
 |
Structure and function of photosystem I with its peripheral antenna systems in green algae and cyanobacteria
Group members working on this project:
Craig Jolley, Devendra Chauhan, Rajagopal Subramanyam
collaboration with:
Nathan Neslon, Adam Ben-Shem, Tel Aviv University
, Israel
Melkozernov, A Chem and Biochem, ASU
and Webber, A.N. , School of Life Sciences (SOLS), ASU |
|
 |
The mechanism of water splitting in PS II investigated by X-ray crystallography and spectroscopy
Group members working on this project:
Ingo Grotjohann, Netra Joshi, Balakumar Thangaraj, HongQi Yu and Christopher Vanselow
cooperation with:
Russel. LeBrutto, ASU, SOLS
and David. Britt, UCLA |
|
 |
Determination of the structure of the proton translocating channel of the ATP Synthase
Group member working on this project :
Ben Varco-Merth
|
| |
 |
Expression folding and structure determination of OEP 16, an amino acid transporter from the Outer Chloroplast Membrane
Group member working on this project:
Daqun Ni
collaboration with:
Ronald Nieman and Douglas A. Klewer, Chem. and Biochem., ASU and
Juergen Soll, MLU Munich
|
|