I-sites
is a library of folding initiation site motif, which are sequence
motifs that correlate with particular local structures such as beta
hairpins and helix caps. I-sites can be used to predict local
structure, or to predict which parts of a protein are likely to fold
early, initiating folding.
For more, see reference [1] and link [1].
I-sites clusters by motif
- Glycine-rich
alpha-N-cap
- Glycine
alpha-C-cap (Schellman) Type 1
- Glycine
alpha-C-cap (Schellman) Type 3
- Diverging
Type-II beta-turn, A
- Amphipathic
alpha helix
- Serine
alpha N-cap (N-capping box), type 1
- Glycine
alpha C-cap, Type 2
- Proline
alpha C-cap
- Alpha-alpha
corner, type 1
- Serine
alpha N-cap, type 2
- DP
alpha N-cap
- Alpha
corner, type 2
- PG
kink
- Type-I
beta hairpin
- Frayed
alpha helix, type 1
- Polar
alpha helix
- Amphipathic
beta strand
- Non-polar
beta strand
- DG
beta hairpin
- Serine
beta hairpin
- Non-polar
alpha helix
- Non-polar
turn
- Frayed
alpha helix, type 2
- Alpha
loop, type 1
- W
loop
- Frayed
non-polar helix
- Diverging
type-II turn, B
- Diverging
type-II turn, C
- Alpha
loop, type 2
- Frayed
alpha helix, type 3
- Miscellaneous
motifs
[References]
- Bystroff, C. & Baker, D.,
Prediction of local structure in proteins
using a library of sequence-structure motifs. J Mol Biol 281, 565-77
(1998).
- de Brevern A.G., Etchebest C. and Hazout S.,
Bayesian probabilistic approach for prediction backbone
structures in terms of protein blocks, Proteins, 41, 271-287 (2000).
- W. Kabsh and C. Sander , Dictionary of protein
secondary structure: pattern recognition of hydrogen-bonded and
geometrical features. Biopolymers 22, 2577-2637 (1983).