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3 a+ S, H" Y% J3 b jVolume 21, Issue 6
, c8 p# a6 q4 X% g+ n0 R6 i( @- eOn the cover: The modeling of protein structures in the complete absence of
+ ^( @0 B0 c5 many sequential similarity to any known three dimensional structure remains a 4 P- j1 p1 m7 s# z& [& X: {6 f: ~
challenging problem. Recently, it has been shown that proteins are built from a 5 f0 e: y6 {9 ~5 W0 ]- [- n
limited set of possible supersecondary structural motifs (Smotif). Menon et al. / t: ]- B9 F. y3 f4 e0 B3 ^
(pp. 891–899) provide a hybrid computational algorithm in which NMR chemical
$ T" C3 ~4 s7 p, i" o2 ?shift information of loop segments is used to guide the selection of entire
$ R3 h! f2 W+ s" p; P% Y' ySmotifs for any given target sequence. The selected Smotifs then assemble into : Z% L/ L/ F) ]* d8 R, w$ u5 T! `5 Q
three dimensional topology. Although the approach usees only backbone fragments 0 Y/ _$ ^2 m. B: S% B4 H& [
of Smotifs without any sequence information and limited experimental ' l7 `/ `, Q% d1 g: O7 P' o- f
information, it is successfully capturing the correct topologies of almost all ! Z7 U* r" V7 s1 k2 K3 p' M: V; O' |
tested targets. The cover image was created by Mario Pujato, graduate student at
5 j# E/ I3 e) |: Nthe Albert Einstein College of Medicine, Bronx, New York.
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发表于 2013-6-10 22:28
