Chapter title |
Automated Protein Structure Modeling with SWISS-MODEL Workspace and the Protein Model Portal.
|
---|---|
Chapter number | 5 |
Book title |
Homology Modeling
|
Published in |
Methods in molecular biology, February 2012
|
DOI | 10.1007/978-1-61779-588-6_5 |
Pubmed ID | |
Book ISBNs |
978-1-61779-587-9, 978-1-61779-588-6
|
Authors |
Bordoli L, Schwede T, Lorenza Bordoli, Torsten Schwede, Bordoli, Lorenza, Schwede, Torsten |
Abstract |
Comparative protein structure modeling is a computational approach to build three-dimensional structural models for proteins using experimental structures of related protein family members as templates. Regular blind assessments of modeling accuracy have demonstrated that comparative protein structure modeling is currently the most reliable technique to model protein structures. Homology models are often sufficiently accurate to substitute for experimental structures in a wide variety of applications. Since the usefulness of a model for specific application is determined by its accuracy, model quality estimation is an essential component of protein structure prediction. Comparative protein modeling has become a routine approach in many areas of life science research since fully automated modeling systems allow also nonexperts to build reliable models. In this chapter, we describe practical approaches for automated protein structure modeling with SWISS-MODEL Workspace and the Protein Model Portal. |
X Demographics
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Unknown | 1 | 100% |
Demographic breakdown
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Members of the public | 1 | 100% |
Mendeley readers
Geographical breakdown
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United States | 2 | 2% |
Turkey | 1 | <1% |
Canada | 1 | <1% |
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Unknown | 119 | 96% |
Demographic breakdown
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Student > Bachelor | 20 | 16% |
Researcher | 17 | 14% |
Student > Master | 13 | 10% |
Professor > Associate Professor | 7 | 6% |
Other | 18 | 15% |
Unknown | 29 | 23% |
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Biochemistry, Genetics and Molecular Biology | 24 | 19% |
Chemistry | 13 | 10% |
Engineering | 7 | 6% |
Physics and Astronomy | 4 | 3% |
Other | 13 | 10% |
Unknown | 34 | 27% |