Tertiary Structure of Proteins. II. Freedom of Dihedral Angles and Energy Calculation
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- Nishikawa Ken
- Institute for Chemical Research, Kyoto University
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- Ooi Tatsuo
- Institute for Chemical Research, Kyoto University
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説明
By using the procedure described in a preceding paper, several sets of \varphi and ψ are obtained which reproduced similar conformations to the native structure of lysozyme or myoglobin. Contrary to the expectation, the value of f has no maximum along a line connected any two of the minima in the 2n-dimensional phase space. This result shows the existence of many solutions for \varphi and ψ which generate the native conformation under restricted condition of fixed geometry in the main chain. Energy calculation is performed on the conformations obtained above to examine atomic collisions along the main chain. After refinement to remove the collisions, a conformation is finally obtained for lysozyme which has a total energy of −270 kcal/mol and still has an low value of f. Similarly a conformation can be found for myoglobin having an energy of −580 kcal/mol in total.
収録刊行物
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- Journal of the Physical Society of Japan
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Journal of the Physical Society of Japan 32 (5), 1338-1347, 1972
一般社団法人 日本物理学会
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詳細情報 詳細情報について
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- CRID
- 1390282679172680960
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- NII論文ID
- 210000082917
- 130003893400
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- BIBCODE
- 1972JPSJ...32.1338N
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- COI
- 1:CAS:528:DyaE38Xls1Wht78%3D
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- ISSN
- 13474073
- 00319015
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- Crossref
- CiNii Articles
- OpenAIRE
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- 抄録ライセンスフラグ
- 使用不可