Recent developments in structural proteomics for protein structure determination.
The major challenges in structural proteomics include identifying all the proteins on the genome-wide scale, determining their structure-function relationships, and outlining the precise three-dimensional structures of the proteins. Protein structures are typically determined by experimental approaches such as X-ray crystallography or nuclear magnetic resonance (NMR) spectroscopy. However, the knowledge of three-dimensional space by these techniques is still limited. Thus, computational methods such as comparative and de novo approaches and molecular dynamic simulations are intensively used as alternative tools to predict the three-dimensional structures and dynamic behavior of proteins. This review summarizes recent developments in structural proteomics for protein structure determination; including instrumental methods such as X-ray crystallography and NMR spectroscopy, and computational methods such as comparative and de novo structure prediction and molecular dynamics simulations.
Liu
Hsuan-Liang
HL
Department of Chemical Engineering, National Taipei University of Technology, Taiwan. f10894@ntut.edu.tw
Hsu
Jyh-Ping
JP
D001230:Aspergillus / Q000201:enzymology; D020134:Catalytic Domain; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D005656:Fungal Proteins / Q000737:chemistry; D008555:Melitten / Q000737:chemistry; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D015221:Potassium Channels / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D040901:Proteomics / Q000639:trends*; D013329:Structure-Activity Relationship
D005656:Fungal Proteins; D015221:Potassium Channels; D011506:Proteins; D008555:Melitten