Lecture 5 - Primary & Secondary structures Flashcards
what makes up backbone of peptide chain
N - C alpha - C unit
what is native conformation
any polypep chain has a single stable shape that it should always fold into, determined by the AA chain
what are the 2 factors that determine protein structure
allowable bond rotation (referring to the psi and phi rotation thing and how some rotations aren’t favourable)
weak non-covalent interactions between the backbone and the side chains
which is more favourbale: cis or trans conformation
trans
cuz cis has steric interference of alpha carbons and their side chains
which AA has restricted rotation around N-C alpha bond
proline
cuz of the fat ring blocking the turn,
so the phi rotation basically cant happen
what does ramachandran plot demonstrate
all combos of psi and phi turns a protein can have, and it shows how some turns are more or less favoured
in an alpha helix, where are the H bonds formed
between C=O (n) and the amide hydrogen of n+4
how is the aplha helix a dipole
the C=O groups point toward C terminus
so N to C is +ve to -ve
what is pitch
length of a whole turn in alpha helix
what is rise
the length occupied by one residue
what can be worked out using the pitch and rise
how many AAs per turn
diff between parallel and antiparallel beta sheets
parallel - the strands are all N-C
antiparallel - stands are alternating N-C
which type of beta sheet is more stable and why
antiparallel more stable
cuz the H bonds are more perpendicular
how are parallel beta sheets connected
have to be connected via a big loop or alpha helix
what characteristic forms the pleated conformation of a beta sheet
R groups will be on alternating surfaces