lecture 3 Flashcards
secondary structure of protein
folding/shaping of a local section of polypeptide
a-helix or beta sheet, beta turn. triple helix, coiled coil
alpha helix
hydrogen bonding helix R groups on outside of helix hydrophobic and hydrophilic part membrane proteins
Alanine- helix forming
Proline- helix breaking
keratin is made from
a helix coiled onto them selves
amino acids that likes B sheet
glycine and alanine
example of protein that is mostly beta sheet
silk- antiparallel - no stretch
example of protein with B barrel
Green fluorescent protein
when full polypeptide folds onto itself
tertiary structure
___ are complexes that help proteins fold correctly, prevent misfolding, uses ATP
chaperones
when multiple polypeptides and subunits combines into final form
quaternary structure
antibodies have two parts and form what
constant and variable part
s-s bridges
explain antibody production
- macrophage eats bacteria, proteins(antigenes) from the bacteria are broken into short peptide chains and displayed on surface
- T cells “see” the peptide on the macrophage and stimulates the B cell to turn on antibody
production - B cells multiply and secrete antibody into plasma. binds to bacteria and flags them to be killed
biological catalysts
enzymes
catalysts ___ reactions
accelerate
exergonic reaction
-(triangle) G
happens spontaneously
endergonic reaction
+(triangle) G
needs help to start reaction