made up about 15% of the cell

*proteins

shape = ?
*amino acid sequence

the proteins are made up of ( how many amino acids? )

*20

the proteins are linked by what?

*peptide bonds

the peptide bonds allows for rotation around it and therefore the protein can fold
and orient the r group in favorable position
*protein folding

weak non covalent interactions will hold the protein in its functional shape. these
are the weak ad will take many to hold the shape
*protein folding

the side chains will help determine the conformation in an aqueous solution
*globular proteins

proteins shape is determined by the sequence of amino acids

*protein folding

proteins shape is determined by the?

*sequence of amino acids

the final shape is called the ?

*conformation

process of unfolding the protein

*denaturation

can be down with heat, ph or chemical compounds

*denaturation

in the chemical compound, can reremove and have the protein renature or refold
*denaturation

small proteins that help guide the folding and can help the new protein from
associating with the wrong partner
*molecular chaperones

2 regular folding patterns that have been identified - formed between the bonds of
the peptide backbone
* alpha helix and beta sheet

protein turns like a spiral fibrous proteins ( hair, nails, horns)

*alpha helix

proteins folds back on in=tself as in a ribbon. globular protein

*beta sheet

core of many proteins

*beta sheet

form rigid structure with the h-bond

*beta sheet

2 types of beta sheet

*anti parallel and parallel

run in an opposite direction of its neighbor

*anti parallel

run in the same direction with longer looping section between them
*parallel

formed by a h-bond between every 4th peptide bond

*alpha helix

usually in proteins that span a membrane

*alpha helix

it can either coil to the right or the left

*alpha helix

it can also coil around each other, coiled coil shape, a framework for structural
proteins such as nails and skin
*alpha helix

4 levels of organization
*primary secondary tertiary quanternary

level of organization, amino acid sequence of the protein

*primary structure

level of organization, h bonds in the peptide chain back bone

*secondary structure

non covalent interactions between the r groups within the protein

*tertiary structure

interaction between 2 polypeptide chains

*quanternary structure

basic structural unit of a protein structure, distinct from those that make up the
conformations
*domain

part of protein that can fold into a stable structure independently

*domain

can have one to many domains depending on protein size

*proteins

usually have only one useful conformation because otherwise it would not be
efficient use of the energy available to the system
*proteins

has eliminated proteins that do not perform a specific function in the cell
*natural selection

multiple peptides
*proteins
can form interactions between indicidual polypeptide chains
*non covalend bonds

where proteins interact with one another

*binding site

each polypeptide chain of large protein

*subunit

protein made of 2 subunits

*dimer

most of what we have dealt so far

*globular proteins

compact shape like a ball with irregular surfaces

*globular proteins

what type of protein is enzyme

*globular

usually span a long distance in the cell

*fibrous proteins

in 3d structure and is usually long and rod shaped

*fibrous proteins

structural scaffold inside the cell

*intermediate filaments of the cytoskeleton

bind cells together to make tissues

*extracellular matrix

secreted from cells and assemble in long fibers

*extracellular matrix

fiber with a glycine every third amino acid in the protein

*collagen

unstructured fibers that give tissue and elastic characteristic

*elastin

family of proteins that can be created to bind to almost any molecule

*antibody family

another term for antibody

*immunoglobulins

made in response to a foreign molecule

*antibodies

bind together tightly and therefore inactivates the antigen or marks it for
destruction
*antibody

important enzyme that protects us from bacteria by making holes in the bacterial
cell wall and causing it to break
*lysozyme
adds h20 to the glycosidic bond in the cell wall
*lysozyme

lysozyme holds the polysaccharide in a position that allows the h2o to break the
bond
*transition state

state between substrate and product

*transition state

is a special binding site in enzymes where the chemical reaction takes place
*active site

non covalent bonds hold the polysaccharide in the active site until the reaction
occurs
*lysozyme