Professional Documents
Culture Documents
Secondary Structure
Motifs and Protein Domains
Laksmi Ambarsari
I
Supersecondary Structure
Motifs of Proteins
Types of Secondary Structure
Types of Secondary Structure
-helix 310 helix -helix
alpha helix,
distabilkan oleh ikatan
Hidrogen
Psi () the
angle of
rotation about
the C-C bond.
Phi () the
angle of
rotation about
the N-C bond.
alpha 3.10 pi
Ik. H 310-helix,
Ikatan H antara (C=Oi ...
H-Ni+3)
Ik. H -helix,
Ikatan H antara (C=Oi ...
H-bonding H-Ni+5)
Ik. H -helix,
amino acids Ikatan H antara (C=Oi ...
per turn: 3.6 3.0 4.4 H-Ni+4)
frequency ~97% ~3% rare
Perbedaan , 3 , - Helix
Perbedaan , 310 , - Helix
10
-turn 2 NH(i)-CO(i+1)
-turn 3 CO(i)-NH(i+2)
-turn 4 CO(i)-NH(i+3)
-turn 5 CO(i)-NH(i+4)
-turn 6 CO(i)-NH(i+5)
Loops
Loops
Connect the
secondary structure
elements.
Have various length
and shapes.
Loops are typically
longer, they are
often called coils and
do not have a
regular or
repeating structure Located at the surface of the
folded protein and therefore
may have important role in
biological recognition
processes.
Loops often have polar aa
Preferred
PreferredResidues forSheet
Residuesfor Sheetand
andTurns
Turns
Handedness
Leucine-rich Motifs
Two-domain protein.
Proteins Domains
Bundle structural domain
Protein1
Protein2
Protein3
Open / /horseshoe
Sheet Fold
(Domain) Folds of Protein
Terimakasih
Terimakasih