SAAP力場 : 単一アミノ酸ポテンシャルを利用した新しいタンパク質力場の開発
スポンサーリンク
概要
- 論文の詳細を見る
The force field of a protein is an important and fundamental tool for protein scientists in modeling the structures. Although currently available all-atom protein force fields have been well tuned, it is still a difficult and time-consuming task to quantitatively reproduce the thermodynamic parameters by computer simulation, especially in water. In this article, a new all-atom protein force field (named as the SAAP force field) , which is based on a novel idea to compose a protein force field by using single amino acid potential (SAAP) functions, is presented.
- 日本生物物理学会の論文
- 2004-03-25
著者
関連論文
- 東海大学における現職理科教員を対象とした研修プログラムの開発と実践
- Synthesis of Diaryl Diselenides Having Chiral Pyrrolidine Rings with C_2 Symmetry. Their Application to the Asymmetric Methoxyselenenylation of trans-β-Methylstyrenes
- Asymmetric Oxyselenenylation of Olefins Using Optically Active Selenobinaphthyls and d-Menthol as a Nucleophile
- 二価有機セレンの非結合性相互作用に関する研究
- 大学前期課程における化学実験のマイクロスケール化(マイクロスケール実験の広場(その 16))
- Weak Nonbonded S…X(X = O, N, and S) Interactions in Proteins. Statistical and Theoretical Studies
- Statistical Characterization of Nonbonded S・・・O Interactions in Proteins
- Characterization of an Intramolecular Nonbonded Interaction between Selenium and Fluorine in Solution
- Deuterium-Induced Isotope Effects of a C-H・・・Se "Hydrogen Bond" on the IR and NMR Spectra of 6H,12H-Dibenzo[b,f][1,5]diselenocin
- SAAP力場 : 単一アミノ酸ポテンシャルを利用した新しいタンパク質力場の開発
- 高選択的かつ高効率的なペプチドSS結合の生成試剤
- 16族元素が関与する弱い原子間 相互作用の定量評価とその応用