| Literature DB >> 28986782 |
Abstract
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 the following 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.Keywords: Comparative modeling; Fold assignment; Model assessment; Multiple templates; Sequence-structure alignment
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Year: 2017 PMID: 28986782 DOI: 10.1007/978-1-4939-7231-9_4
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745