Comparative modeling for protein structure prediction.
With the progression of structural genomics projects, comparative modeling remains an increasingly important method of choice. It helps to bridge the gap between the available sequence and structure information by providing reliable and accurate protein models. Comparative modeling based on more than 30% sequence identity is now approaching its natural template-based limits and further improvements require the development of effective refinement techniques capable of driving models toward native structure. For difficult targets, for which the most significant progress in recent years has been observed, optimal template selection and alignment accuracy are still the major problems.
Ginalski
Krzysztof
K
Centre for Mathematical and Computational Modelling, Warsaw University, Pawińskiego 5a, 02-106 Warsaw, Poland. kginal@icm.edu.pl
D000465:Algorithms; D029968:Escherichia coli Proteins / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry; D008958:Models, Molecular; D009601:Nitroreductases / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D020539:Sequence Analysis, Protein; D040681:Structural Homology, Protein; D020124:Thermotoga maritima / Q000201:enzymology
D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D011506:Proteins; C489181:tonB protein, E coli; D009601:Nitroreductases