catalyzing chemical reavrions
providing structural support
transporting substanves im the body
ensbling organisms to move
regulating cellular processes
providing defence from disease
amylase, hemoglobin, fibrin, collagen, actin, growth hormone, potassium channels, insulin
a macromolecule composed of amino acid monomers joined by a peptide bond
hydrogen, amino group, carboxyl, r group
8-10
a polymer composed of many amino acids linked together
primary, secondary, teritary, quaternary
linesr sequence of amino acuds
peptide bonds are polar
so h-bond occurs
polypeptides form coil
like shape caleld alpha helix or a folded fan shape called beta pleated sheet
secondary
complex process of folding
most occur naturally by peptide bonds and sifferent R groups interact
happens by hydrophobic effect
may involve assistance of proteins called molecular chaperones
made up combinaiton of polypeptides each with their own primary secondsry and tertiary atructures
under certain conditions(extreme tempersture) proteins can unfold
once a protein unfolds it no lomger has its function
amino and carboxyl
all amino acids have the smae structure so the disctinvtive shape and properties come from the r group
because rhere are 20
amino acids which results in way more possibilites for unique chains
carries oxygen in our blood
givea structure and supports pur slim, tendon and even bones
helps send signals theough the brain and other nerve cells
refulates the amount of sugar in the blood and is used to treat diabieyes
forms a scan to protect cuts as they heal
transforms alcohol into a non-todic form that the body ises for food
20