2011 - 11 句子精選
2011 - 12 蛋白質結構
2012 - 01 Performance
2012 - 02 Free energy
2012 - 03 Salt-bridge
2012 - 04
2012 - 05 Delphi
2012 - 06 Thermophilic and interface
2012 - 07 隨意 再分類
2012年7月24日 星期二
Conservation Score 寫法
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Conservation scores of residues
In our study of TIM-barrel proteins (11), we have used the following conditions to predict the SRs: (i) HP ≥ 20 kcal/mol; (ii) LRO ≥ 0.02; (iii) SC ≥ 1; and (iv) conservation score ≥ 6.
Conservation scores of residues
Conservation of residues is identified by comparing the sequence of PDB (14) entries with sequences deposited in Swiss-Prot (15) using a local implementation of the public server ConSurf (10) (http://consurf.tau.ac.il). The ClustalW (17) aligned homologous sequences found by PSI-BLAST (19) are used to calculate the measure of conservation by the Rate4Site algorithm (20). Residues are classified into nine categories according to their real conservation score. A score of 1 represents the most
variable residues and a score of 9 represents the most conservative ones.
In our study of TIM-barrel proteins (11), we have used the following conditions to predict the SRs: (i) HP ≥ 20 kcal/mol; (ii) LRO ≥ 0.02; (iii) SC ≥ 1; and (iv) conservation score ≥ 6.
2012年7月22日 星期日
Surrounding hydrophobicity
The experimental values are given below:
Ala Asp Cys Glu Phe Gly His Ile Lys Leu Met Asn
0.87 0.66 1.52 0.67 2.87 0.10 0.87 3.15 1.64 2.17 1.67 0.09
Pro Gln Arg Ser Thr Val Trp Tyr
2.77 0.00 0.85 0.07 0.07 1.87 3.77 2.67
Form
1. Book ( Google book)
Protein Bioinformatics From Sequence to Function

2. Papers: Nature 1978 Manavalan
Ala Asp Cys Glu Phe Gly His Ile Lys Leu Met Asn
0.87 0.66 1.52 0.67 2.87 0.10 0.87 3.15 1.64 2.17 1.67 0.09
Pro Gln Arg Ser Thr Val Trp Tyr
2.77 0.00 0.85 0.07 0.07 1.87 3.77 2.67
Form
1. Book ( Google book)
Protein Bioinformatics From Sequence to Function
2. Papers: Nature 1978 Manavalan
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