The influence of tertiary structure on secondary structure prediction

FEBS Letters

Taylor, William R.¹  Thornton, Janet M.¹  Garratt, Richard C.¹ 

[1] Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, London WC1E 7HX, England

关键词: Secondary structure prediction;    β-Sheet residue;    Tertiary structure;    Solvent accessible area;    Residue hydrogen bonding;   

DOI  :  10.1016/0014-5793(85)80874-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The secondary structure prediction algorithm of Garnier et al. [(1978) J. Mol. Biol. 120, 97-120] has been used for 16 proteins whose structures are dominated by β-sheet. Comparisons of the predicted structures with those defined by the algorithm of Kabch and Sander [(1983) Biopolymers 22, 2577-2637] shows that for β-sheet residues, the quality of prediction falls markedly with increasing residue accessibility. 2 sub-classes of β-residues have been distinguished on the basis of hydrogen bonding patterns, and the distribution of amino acid types within each sub-class found to be quite different. Accordingly, Chou and Fasman P _β-type parameters for these previously indistinguished states have been derived.

【 授权许可】

Unknown