Title |
ROTAS: a rotamer-dependent, atomic statistical potential for assessment and prediction of protein structures
|
---|---|
Published in |
BMC Bioinformatics, September 2014
|
DOI | 10.1186/1471-2105-15-307 |
Pubmed ID | |
Authors |
Jungkap Park, Kazuhiro Saitou |
Abstract |
Multibody potentials accounting for cooperative effects of molecular interactions have shown better accuracy than typical pairwise potentials. The main challenge in the development of such potentials is to find relevant structural features that characterize the tightly folded proteins. Also, the side-chains of residues adopt several specific, staggered conformations, known as rotamers within protein structures. Different molecular conformations result in different dipole moments and induce charge reorientations. However, until now modeling of the rotameric state of residues had not been incorporated into the development of multibody potentials for modeling non-bonded interactions in protein structures. |
X Demographics
Geographical breakdown
Country | Count | As % |
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Unknown | 2 | 100% |
Demographic breakdown
Type | Count | As % |
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Scientists | 2 | 100% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
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United Kingdom | 1 | 3% |
Unknown | 29 | 97% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 10 | 33% |
Researcher | 6 | 20% |
Student > Bachelor | 3 | 10% |
Other | 3 | 10% |
Student > Postgraduate | 2 | 7% |
Other | 5 | 17% |
Unknown | 1 | 3% |
Readers by discipline | Count | As % |
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Agricultural and Biological Sciences | 9 | 30% |
Chemistry | 7 | 23% |
Computer Science | 5 | 17% |
Biochemistry, Genetics and Molecular Biology | 3 | 10% |
Engineering | 2 | 7% |
Other | 0 | 0% |
Unknown | 4 | 13% |