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Volume 21, Issue 6
. f* T9 g& C, F n$ \On the cover: The modeling of protein structures in the complete absence of $ D4 V+ X. L8 a
any sequential similarity to any known three dimensional structure remains a
' S! Z, u" ~0 C5 Ichallenging problem. Recently, it has been shown that proteins are built from a ) J, P# c- U) P9 G6 s0 Q% Q
limited set of possible supersecondary structural motifs (Smotif). Menon et al. + G P6 \6 |) p
(pp. 891–899) provide a hybrid computational algorithm in which NMR chemical " E, |% e. [ ^; C& H/ D: G3 w2 c3 x
shift information of loop segments is used to guide the selection of entire ! f9 H: o) m2 h8 A! N3 Q9 ~" @+ G8 T
Smotifs for any given target sequence. The selected Smotifs then assemble into
" ?! j( p% ^1 g+ F" x& w2 u# q9 ~three dimensional topology. Although the approach usees only backbone fragments / c6 @+ d. R0 Y7 F6 q7 G5 E
of Smotifs without any sequence information and limited experimental & p+ G3 B G+ U4 c4 \
information, it is successfully capturing the correct topologies of almost all
9 E6 b: K }& d4 S8 }4 z4 dtested targets. The cover image was created by Mario Pujato, graduate student at 6 S( c/ q4 h6 y C/ M! J' I0 }
the Albert Einstein College of Medicine, Bronx, New York.
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发表于 2013-6-10 22:28
