Genome sequencing projects have resulted in a rapid increase in the number of known protein sequences. In contrast, only about one-hundredth of these sequences have been characterized at atomic resolution using experimental structure determination methods. Computational protein structure modeling techniques have the potential to bridge this sequence–structure gap. In this chapter, we present an example that illustrates the use of MODELLER to construct a comparative model for a protein with unknown structure. Automation of a similar protocol has resulted in models of useful accuracy for domains in more than half of all known protein sequences. Key
CITATION STYLE
Källberg, M., Margaryan, G., Wang, S., Ma, J., & Xu, J. (2014). Chapter 2 RaptorX server : A Resource for Template-Based. Methods in Molecular Biology, 1137(April), 1–15.
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