Igor Tuk

Period 6
Proteins
1. Enzyme a macromolecule serving as a catalyst, a chemical agent that increases the rate
of a reaction without being consumed by the reaction; mostly proteins
2. Catalyst a chemical agent that selectively increases the rate of a reaction without being
consumed by the reaction
3. Polypeptides a polymer of many amino acids linked together by peptide bonds; proteins
with peptide bonds
4. Proteins biologically functional molecule consisting of one or more polypeptides folded
and coiled into a specific three-dimensional structure
5. Enzymatic proteins to promote chemical reactions that synthesize or break apart
biological molecules without being changed themselves
6. Structural proteins- provides scaffolding or something that give the cell or one of it's
organelles shape; mostly fibrous proteins
7. Storage proteins- main function to store metal ions such as iron in your body; body needs
iron to transport hemoglobin for cell metabolism.
8. Transport proteins- like the name suggests, transport items through the body;
Hemoglobin brings oxygen to your lungs and tissues
9. Hormonal proteins- hormones found in the endocrine glands; peptides,steroids.
10. Receptor proteins- located at the exterior of the cell plasma membrane and regulate
substances and nutrients in and out of your cells
11. Contractile proteins-control contractions in the heart and muscles (regulate the speed and
strength of the contractions)
12. Defensive proteins-antibodies that help your immune system fight off disease (antibodies
are made in your white blood cells and bind to viruses and bacteria)
13. Amino acids an organic molecule possessing both a carboxyl and an amino group;
serve as the monomers of polypeptides
14. Peptide bond the covalent bond between the carboxyl group on one amino acid and the
amino group on another, formed by a dehydration reaction
15. Primary structure the level of protein structure referring to the specific linear sequence
of amino acids
16. Secondary structure regions of repetitive coiling or folding of the polypeptide backbone
of a protein due the hydrogen bonding between constituents of the backbone
17. Alpha helix a coiled region constituting one form of the secondary structure of proteins,
arising from a specific pattern of hydrogen bonding between atoms of the polypeptide
backbone
18. Beta pleated sheet one form of the secondary structure of proteins in which the
polypeptide chain folds back and forth; two regions of the chain lie parallel to each other
and are held together by hydrogen bonds between atoms of the polypeptide backbone
19. Tertiary structure the overall shape of a protein molecule due to interactions of amino
acid side chains, including hydrophobic interactions, ionic bonds, hydrogen bonds and
disulfide bridges
20. Hydrophobic interaction a type of weal chemical interaction caused when molecules
that do not mix with water coalesce to exclude water
21. Disulfide bridges a strong covalent bond formed when the sulfur of one cysteine
monomer bonds to the sulfur of another cysteine monomer. \
22. Quaternary structure the particular shape of a complex, aggregate protein, defined by
the characteristic three-dimensional arrangement of its constituent subunits, each a
polypeptide
23. Denaturation a process in which a protein loses its native shape due to the disruption of
weak chemical bonds and interaction, thereby becoming biologically inactive
24. Chaperonins- protein complex that assists in the proper folding of other proteins
25. Hydrogen bonding type of weak chemical bond that if formed when the slightly
positive hydrogen atom of a polar covalent bond in one molecule is attracted to the
slightly negative atom of a polar covalent bond in another molecule or in another of the
same molecule.

1. A.
2. D.
3. A.
4. A
5. A
Learning Objective
1. A amino acid is a carbon at the center with an amino group to the left, a carboxyl group
to the right, a side chain known as the R group on top, and a hydrogen below. The R
group is what changes between the numerous amino acids. Cells use 20 of these amino
acids to make up the thousands of proteins needed in the body. The characteristics of the
amino acid rely on the R group, which affects its functional role in a polypeptide. This R
group is what makes the amino acid basic or acidic since its the only difference between
the amino acids.
2. Non-essential amino acids are the ones the body can synthesize and produce by its own.
However, essential amino acids are the ones the body cannot synthesize on its own and is
received from food. There are 20 essential amino acids for humans, which of course we
get from our diet.

3. Amino acids can be polar or non-polar, which is determined by the R group attached to
the central carbon. Amino acids with basic R groups have a positive charge while acidic
have a negative charge, which makes the entire amino acid positive or negative. In turn,
this makes the amino acid polar and hydrophilic.
4. Amino acids can come in two forms: L or D, depending on the arrangement around the
central carbon. L and D form is the same as left-handed and right-handed configurations,
which makes it easier to visualize. Although both have the same chemical makeup,
mostly L form is active in biological systems.
5. A dehydration reaction bonds two amino acids together through the removal of water.
One amino acid gives up an H while the other gives up an OH. The resulting covalent
bond is called a peptide bond. Multiple dehydration and peptide bonds form a
polypeptide from amino acids. A polypeptide can be broken down through condensation
reaction, which is when the peptide bond gets broken with water and the amino acids
become separate.


6. The primary structure of proteins is a linked series of amino acids with a unique
sequence. The precise structure is determined by inherited genetic information, not
random linkages of amino acids. The primary structure dictates secondary and tertiary
structure due to the chemical nature of the backbone and side chains. On the other hand,
the secondary structure is the repeatedly coiled or folded patterns in the segments of the
polypeptide chain which contribute to the proteins overall shape. These coils and folds
are the result of hydrogen bonds between the repeating constituents of the polypeptide
backbone. The first main type is the helix, which is a coil held together by hydrogen
bonding on every fourth amino acid. The other is pleated sheets which is two or more
strands of polypeptide chain lying side by side are connected by hydrogen bonds between
parts of the two parallel polypeptide backbones. These make up the core of many
globular proteins.
7. Tertiary structure is the overall shape of a polypeptide resulting from interactions
between the side chains of the various amino acids. A hydrophobic interaction can occur
which is caused by the exclusion of nonpolar substances by water molecules. In turn, van
der Waals interaction will help the nonpolar amino acid side chains stick together. In
addition, disulfidge bridges reinforce the shape of protein when two cysteine monomers
are brought close together by the folding of the protein. The sulfur of one bonds to the
sulfur of the other and the disulfide bridge rivets parts of the protein together.
8. Globular protein is easily water soluble while fibrous is insoluble. In addition, globular
has polypeptide chains that are folded into a spherical shape while fibrous has parallel
polypeptide chains in long fibers or sheets. Globural proteins can be catalytic such as
enzymes, or regulatory such as hormones like insulin, or transport like hemoglobin, or
even protective like antibodies. On the other hand, fibrous proteins can have a structural
role like collagen, or contractile.
9. Hydrogen bond is when hydrogen bonds to either oxygen or nitrogen, which makes
helix or helix. This of course happens in the secondary structure of proteins. Ionic
bonds have a charged R group above the central carbon in amino acids, which interacts in
the tertiary and quaternary structure. Disulfide bonds makes a disulfide bridge between
the sulfurs of two cysteine bonds and rivets parts of the protein together, which occurs at
the tertiary structure. Hydrophobic interaction involve nonpolar R groups attached to the
central carbon in amino acids, which affects the tertiary or quaternary structure.
10. Denaturation is when a protein unravels and loses its native shape due to a destruction of
the weak chemical bond. pH, salt concentration, temperature or other aspects of the
environment can cause denaturation. Most proteins become denatured if they are taken
from an aqueous environment to a nonpolar solvent. Since the protein is misshapen, it
becomes biologically inactive.
11. Quaternary structure is the overall protein structure that results from the aggregation of
these polypeptide subunits. Simply its two or more polypeptide chains together in a
protein. For example, hemoglobin is made up of a total of four subunits, two with alpha
helix and two with beta helix. Each subunit has a nonpolypeptide component with an iron
atom that binds to oxygen, giving it the ability to transport oxygen through the body.