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polypeptides structure
unbranched polymers built from the same set of 20 amino acids
structure of amino acids
alpha carbon (central carbon), R group, carboxyl group, amino group
categories of amino acids
nonpolar or polar side chains
Nonpolar side chains
methyl, C, H, no oxygens or nitrogens
Polar side chains
hydroxyl, amino, suflhydryl could be at the end (hydrogen bonded to more electronegative things so it’s more attracted to water forming hydrogen bonds)
polypeptides bond during dehydration synthesis
peptide bonds
polypeptide’s size range
few to more than a 1000 monomers
structure of polypeptides
carboxyl end + unique linear sequence of amino acids + amino end
how do peptide bonds form in polypeptides
carboxyl end gives Oh and amino group gives H they join to make water and water is removed to join them together through dehydration synthesis
protein structure
1 or more polypeptides twisted, folded, and coiled
What determines how proteins fold?
Order of amino acids
What determines proteins function?
structure
Four levels of protein structure
primary, secondary, tertiary, quaternary
Primary function
sequence of amino acids (alpha felix)
Primary level function
different side chains join to make a long polypeptide chain + amino end + carboxyl end
Secondary level structure
coils and folds in polypetide chains because of backbone interactionsS
Secondary level function
hydrogen bonding between various parts of the backbone (carbon, carboxyl joined to hydroxyl, alpha carbs so they lead alpha helix shape and beta plated sheet,; hydrogen which used to be a part of amino bonded to oxygen double bonded to one carboxyl group)
Tertiary structure
interaction of R groups
Tertiary function
could have hydrogen bonds, hydrophobic interactions, covalent bonds, or ionic bonds
Quaternary structure
structure when protein consists of multiple polypeptide chains
4 identical polypeptides
Quaternary function
carboxyl end gives Oh amino group gives H joins to make water so peptide bonds are formed