Motifs Flashcards
Importance of structure irregularity
helps proteins fulfill diverse functions, able to recognize thousands types of molec
Interior of proteins
hydrophobic core
Driving force of folding water soluble proteins
To pack HPhob side chains into interior of molec
Folding HPhob side chains into center -> main chain (polar/HPhil due to -NH and -COOH groups) must fold into center as well; how to stabilize?
secondary structures: forms H-bonds to neutralize polarity, forms btwn H of the -NH and carbonyl oxygen of the -COO
Residues per turn in A helix
3.6 residues (5.4 A)
Angstroms per turn in A helix
3.6 residues/5.4 A = 1.5 A
In A helices, H bonds form every
4th AA, btwn n and n+4
Ends of A helices are
polar, almost always towards surface
Why are the ends of A helices more polar?
first -NH group and last -COO group not H bonded
how are H bonds in A helices oriented?
parallel to helical axis, between nearby residues, forms btwn H of the -NH and carbonyl oxygen of the -COO
how are side chains in A helices oriented?
perpendicular to helical axis
Why does A helix exhibit a dipole moment?
peptide units and H bonds aligned in the same orientation as helical axis, peptide bonds have dipole (N term is pos, C term is neg), whole helix has a macroscopic dipole moment
ligands attracted to N terminus of A helix
negative groups, especially phosphate groups
preferred AA’s in A helices
small HPhob residues, eg Ala, Leu (other good choices are in Tooze 17)
helix breakers
Pro, Gly (other bad choices are in Tooze 17)
Why is Pro is helix breaker?
rotation around the N-Ca bond is impossible
Why is Gly is helix breaker?
tiny R-group supports other conformations
how are H bonds in B sheets oriented?
perpendicular to the direction of the strand, between dif strands, forms btwn H of the -NH and carbonyl oxygen of the -COO