Bio 201 Lessons 3-4

Structure resulting from two or more protein subunits assembling to form a larger, biologically active protein complex

Structure that describes the alpha-helices and beta sheets that are formed by hydrogen bonding between backbone atoms located near each other in the polypeptide chain

What two functional groups are always found in amino acids?

What structural features makes the 20 common amino acids different from one another?

What type of interaction stabilizes the alpha helix and the beta-pleated sheet structures of proteins?

What type of bonds is a disulfide bridge?

True or False: If we changed a single amino acid in a protein consisting of 433 amino acids, the primary structure is always altered but the tertiary structure is only altered sometimes

Inhibitor that has a structure that is so similar to the substrate that it can bond to the enzyme just like the substrate

Inhibitor that binds to a site on the enzyme that is not the active site

Inhibitor that forms a covalent bond with an amino acid R group within the active site, which prevents the substrate from entering the active site or prevents catalytic activity

What kind of bonds are formed when an amino acid R group interacts with an irreversible inhibitor?

The competitive inhibitor competes with the substrate for what location on the enzyme?

When the noncompetitive inhibitor is bonded to the enzyme, what happens?

Enzyme inhibitors disrupt normal interactions between an enzyme and its...

What can you do to regain the activity of an enzyme after adding an irreversible inhibitor?

What can you do to speed up a reaction again after adding a competitive inhibitor?

What mechanism regulates enzyme activity in eukaryotic cells?

Reaction in which amino acids are joined together as the carboxyl group of one is adjacent to the amino group of the other

What kind of bond is formed by a dehydration reaction and two amino acids being joined together?

Model used to show the 3-D shape of a protein including all of the atoms composing it

Diagram used to show the general shape of a protein along with some important functional details such as folds and coils

Model used to show the 3-D shape of a protein including the backbone structure, folds, and coils

Shape used to show a generalized protein in which the focus is on the protein's function rather than its structure

Model used to show the 3-D shape of a protein by showing the amino acid R groups and their interactions

True or False: Each protein has a unique linear sequence of amino acids

What are the 4 categories of amino acids?

What polymers make up proteins?

The secondary structure of a protein results from what types of bonds?

True or False: Tertiary structure is directly dependent on peptide bonds

True or False: Hydrogen bonds are involved in secondary, tertiary, and quaternary structure

True or False: All proteins have primary, secondary, and quaternary structures but not necessarily tertiary structure

What kinds of bonds are holding quaternary structures together?

True or False: The R group is involved in determining the secondary structure of protein

Secondary structures are driven by interactions with the peptide backbone, so what kinds of amino acids can participate?

What types of interactions are major drivers of protein folding for many proteins?

True or False: Amino acids far apart in primary structure may interact in tertiary structure

What determines the 3-D shape of a protein?

True or False: The ionized amino group is positive while the ionized carboxyl group is negative

What are the four main chemical interactions that stabilize tertiary structures when involving R groups?

True or False: Disulfide bonds are weak in an aqueous environment

True or False: Electrostatic Interactions, Hydrogen Bonds, and Hydrophobic Interactions are weak in aqueous environments

Where do amino acids join a growing end of a polypeptide chain?

Process in which proteins unravel and lose their shape; primary structure left in intact, but the protein is not folded and usually not functional

What level of protein structures are disrupted by protein denaturation?

How many polypeptides make up an antibody?

Region unique to each antibody and can recognize a unique structure (often recognizing another protein involved in pathogenic infection)

What kinds of interactions occur with an antibody's variable region and the specific part of an antigen it recognizes?

What levels of protein structures are covalent bonds such as peptide bonds and disulfide bonds found?

What levels of protein structures are hydrogen bonds between R groups found?

What levels of protein structures are ionic bonds found?

What levels of protein structures are hydrophobic interactions found?

What determines protein function?

True or False: A protein can perform multiple functions it it has multiple domains

Distinct function and/or structural units in a protein; usually responsible for a particular function or interaction, contributing to the overall role of a protein

A protein that catalyzes a specific chemical reaction and remains unchanged itself

A molecule that is converted to products by enzymatic catalysis

Region of the protein that binds and acts upon the substrate

What types of surfaces allow for specific protein-protein interactions?

True or False: The same noncovalent interactions that stabilize protein tertiary structures also mediate interactions between proteins

Enzyme reactions are predominantly organized in pathways where the products of one enzyme are _______ for the next

What happens when a mutation occurs on the active site?

Technique used to make point mutations to determine which amino acids are essential in specific protein functions (function linked to structure)

Technique when pure protein is crystallized, exposed to x-ray beams and the diffraction pattern ultimately determines the overall structure of a protein (structure linked to function)

True or False: Protein domains can involve tertiary and quaternary structures