Influence of medium and long range interactions in protein folding

被引:15
作者
Gromiha, MM
Selvaraj, S
机构
[1] Inst Phys & Chem Res, Riken Life Sci Ctr, Tsukuba, Ibaraki 3050074, Japan
[2] Bharathidasan Univ, Dept Phys, Tiruchirappalli 620024, India
关键词
D O I
10.1080/10826069908544933
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Protein structures are stabilized by both local and long range interactions. In this work, we analyze the residue-residue contacts and the role of medium and long-range interactions in globular proteins belonging to different structural classes. The results show that while medium range interactions predominate in all-alpha class proteins, long-range interactions predominate in an-beta class. Based on this, we analyze the performance of several structure prediction methods in different structural classes of globular proteins and found that all the methods predict the secondary structures of all-alpha proteins more accurately than other classes. Also, we observed that the residues occurring in the range of 21-30 residues apart contributes more towards long-range contacts and about 85% of residues are involved in long-range contacts. Further, the preference of residue pairs to the folding and stability of globular proteins is discussed.
引用
收藏
页码:339 / 351
页数:13
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