U7 - a + b
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what type of amino acids link by a peptide bon
L
what is the N terminus
the beginning is signaled by the presence of a free amino group on the left hand side of the chain
what is the c terminus
the end of a chain is signaled by the presence of a free COOH group on the right hand side of the chain
what kind of bond is the peptide bond similar to and why
double bond. it’s essentially planar since the max rotation is 6 degrees
how are the carboxyl oxygen and amino hydrogen across a double bond situated
trans
what causes the primary structure to twist
L chiral form of amino acids and steric hindrance
what stabilizes the alpha helix
hydrogen bonding
what interact in an alpha helix
the carbonyl oxygen and the hydrogen on a nitrogen 4 amino acids down the chain
how many AA involved an 1 turn
3.6
what is the sequence that forms an alpha helix
-P-N-P-P-NN-P
what cant form an alpha helix
proline and hydroxyproline
what stabiizes the beta sheet
hydrogem bondin
how many AA involved in a beta sheet
5-15
what sequence forms a beta sheet
-N-P-N-P-N-P-N
what are the forms of the beta sheet and which is more stable
parallel and antiparallel *
what stabilizes the suprahelix
hydrogen bonds supplied by glycine
basic unit of suprahelix
tropocollagen
what is a suprahelix
3 identical macromolecules intertwined
what type of protein does a suprahelix form
structural collagen
why does the protein form a tertiary strucutre
to associate into its lowest free energy form
what kind of interactions are involved in the tertiary structure
hydrophobic interactions electrostatic bonds between opposite charges hydrogen bonding covalent disulfide links
what is the quaternary structure and what 3 things can it form
2 or more tertiary globular proteins associating into dimers, tetramers, or octamers
what are the 2 most important simple proteins to food scientists
albumins and globulins
what are albumins soluble in
neutral distilled water