Hideaki Moriyama
Research Associate Professor
Hamilton Hall 29B
402.472.5367
hmoriyama2@unlserve.unl.edu
Moriyama Research Group
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Recent Publications
Figure 1 – A dUTPase crystal
Current Research
Relationships between planetary-scale changes in the environment and biological adaptation are of important concern. The long-term goal of in my lab is to elucidate mechanisms of biological adaptation and to predict the future form of organisms through the atomic description of biological macromolecules. To approach this goal, we are proposing a concept of "temperature driven evolution," in which I try to organize information and to model the biological system along physical factors including temperature.
Figure 2 – A dUTPase structure
The temperature optima of enzymes are the consequence of trade-offs between chemical reactivity and stability of proteins. Therefore I consider an enzyme representing organisms but not simply as a catalyst. Ideally thermodynamics should be introduced to describe the temperature optima. However, for now, I have been using variable temperatures and a fixed pH as primary factors; and pressure, volume, mass as co-primary factors. It is due to the complexity of protein behaviors.
Figure 3 – Sea star, materials
The physiological studies of enzymes are performed at fixed temperatures as an environmental factor and variable pH. Since signals are transmitted by a change of pH and a change of ion level such as calcium, investigating proteins as a function of pH is almost equal to reconstructing reception of signals upon stimulation. Information flow in an organism contains at least two categories: electrical signal transduction and chemically-programmed phase transitions. Sensory cells and sperm cells convert stimulations into electrical signals, which is the digital code in the brain, using signal transducing proteins and ion-channels. The proteins that are involved in these processes are particularly interesting since they serve as cellular messengers and regulators of signal processing.
Figure 4 – X-Ray diffractometer
Because of the nature of protein crystallography, unavoidable obstacles exist including crystallization and phase problems. Remarkable developments in synchrotron technology lowered the latter obstacle especially through the use of light atoms as anomalous scatterers. It became possible to bring such technologies to the laboratory level equipment. Use of unique environments, such as microgravity and magnetic fields, would allow better crystallization of proteins. crystallization where the fixed maximum solute is assumed.
- thermodynamics
- protein folding
- protein thermostability
- cellular signaling
- fertilization
- vision
- G protein-coupled receptors
- machine learning
- bioinformatics
- protein molecular modeling
- protein-ligand docking
- proteomics
- evolution
A graduate or postdoctoral student in my group can expect to receive training in chemical biology, molecular biology and structural biology and significant exposure to one or more of the following specialties: protein expression, purification, crystal growth, crystallography, small angle scattering.
