Functional Dynamics of Proteins
1Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 300, Taiwan
2Department of Chemistry, Rice University, Houston, TX, USA
3Institute of Biological Chemistry, Academia Sinica, Taiwan
4College of Nursing and Health Professions, University of Southern Indiana, Evansville, USA
Functional Dynamics of Proteins
Description
Atomic thermal fluctuations and protein domain motions, basic consequence of the definition of temperature, are essential to protein functions. The vibrant nature of proteins poses a challenge to rational drug design where the synthetic chemical probes/drugs have to hit the “moving targets.” “Healthy” protein dynamics, resulting from a delicate interplay between conformational selection and induced fit, are essential to precise enzymatic reactions and molecular recognitions. Atoms in enzymes are believed to function as an interacting network and are therefore allosterically regulated. Molecular motions that could promote catalyzed chemical reactions vary in sizes, from side chain flipping, domain rearrangement, to collective motions that involve the entire protein. The time scales of these motions can span from picoseconds to milliseconds, which calls for variety of spectroscopic technology and simulation schemes to proper address the dynamics occurring in hierarchical time and space.
With the rising interest in protein dynamics that are known crucial to drug design and disease-related protein-protein interaction/recognition, we herein call for manuscripts that report studies revealing the relation between protein dynamics and their functions. Reviews that summarize the advancement of spectroscopic technology and theoretical methods that address the importance of functional dynamics are welcome. Potential topics include, but are not limited to:
- Advanced spectroscopic and theoretical methods that characterize local and global dynamics
- Conformational changes found or predicted in the protein-ligand interactions and how the understandings of protein/ligand dynamics can facilitate the rational drug design
- Structure ↔ dynamics ↔ function relationship reported for a particular system
- Single molecule experiments that report the time and spatial distribution of interesting molecular events
- Nonequilibrium dynamics including protein folding/misfolding/unfolding
- Databases and web servers that store and generate dynamics data of protein, DNA/RNAs, and other biomolecules
- Dynamics and conformational changes that are observed and predicted in the protein-protein interaction and protein-ligand docking
- Discussions and systematic reviews of aforementioned topics (reviews)
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