protiens Flashcards
what makes proteins
amino acids covalently linked w peptide bonds
what is the structure of these amino acids
amino group, alpha carbon, R group, carboxyl group
what is the bond that connects amino acids
peptide bond– to make the bond it releases H20 it connects the carboxyl group and the amino group
what is a key element of the structure of proteins
structural polarity
structural polarity
here are differences to opposite sides of a molecule or cell
which end is the n terminus
the start also the amino group
which end is the c terminus
the carboxyl end and also the real end
why is protein structure important
it determines function
primary structure
is the sequence of amino acids and it determines how the proteins fold
secondary structure
results from interactions w close amino acids and hydrogen bonds a helixs (r groups face out) b sheets
tertiary structure
the 3 dimensional shape of the polypeptide
- folding determines this… hydrogen bonds
- folding determined by amino sequence
quaternary structure
results from interactions of polypeptide subunits
what can a misfolded protein lead to
disease
what disease is caused by misfolded protiens
sickle cell anemia
protein regulation
- gene expression
- physical location
- changes to the shape or surface characteristics (allosteric regulation)
competitive inhibition
when multiple things can fit in to the active site and then maybe a competative inhibitor fits instead of the substrate
allosteric regulation
when a inhibitor goes into a allosteric site which changes the shape of the active site
allosteric activation
when a inhibitor goes into a allosteric site which changes the shape of the active site so that the substrate can fit
allosteric inhibition
when a inhibitor goes into a allosteric site which changes the shape of the active site so that the substrate can not fit in
what are the three different types of amino acids
hydrophobic, hydrophilic, and special amino acids
what is an example of a hydrophobic amino acid
Alinine
special amino acid example?
Proline
hydrophilic amino acid example?
Threonine
Disulfide bonds
formed between the thiol groups of cysteine residues by the process of oxidative folding
