Chemistry

Front 1

1. non-polar aa's normally have what as side chains?
2. polar neutral?
3. polar acidic?
4. polar basic?
5. what chirality is used exclusely in humans?

Back 1

1. hydrocarbon or thioether
2. amide, alcohol, and phenol
3. carboxilic acid
4. amide
5. L-isomer

Front 2

1. what is the zwitterion form of amino acids?
2. when the overall charge is zero, what is that called?
3. Oligopeptide has how many aa?
4. polypeptide?
5. protein?

Back 2

1. when the amino acids there is a positive charge on the amine and a negative charge on the carboxylic acid.
2. isoelectric point
3. 10-20
4. 20-50
5. 50 or more

Front 3

1. individual aa's in a polypeptide or protein are called
2. what is the N terminal?
3. C-term?
4. the identical repeating structures are called what of the protein?
5. what does the seqence of the side chains determine?

Back 3

1. residues
2. the aa with the free unconnected amino group
3. the aa with the free unconnected carboxylic acid group
4. backbone
5. 3d structure of a peptide or protein

Front 4

1. what is enkephalins?
2. what does glutathione do?
3. what is the sequence of aa in the protein called?
4. what is the secondary structure? (2 major structure)

Back 4

1. neurotransmitters in the brain to reduce pain perception
2. protects structures from oxidation
3. primary structure
4. the repeating patterns of folding that occurs because of HYDROGEN BONDING bt peptide bonds. (alpha helix and beta pleated sheet

Front 5

1. 4 types of side chain interactions (strongest to weakest)

Back 5

1. salt bridge, disulfide bridges, hydrogen bonding and hydrophobic

Front 6

1. when can you have a disulfide bridge?
2. when can you have a salt bridge?
3. when can you have a hydrogen bonding?
4. hydrophobic interactions?
5. refers to the proteins that contain 2 or more polypeptide chains that are independent of each other

Back 6

1. bt 2 cysteine residues (2 SH groups)
2. positively charged polar basic aa and one negatively polar aciding aa
3. bt 2 polar neutral
4. bt 2 non-polar side chains (most important)
5. quaternary structure

Front 7

1. when are disulfide useds?
2. fibrous proteins are what? water solublity?
3. globular proteins are what? water solublity?
4. what is a keratin? shape? how are they strengthed?
5. the most abundant protein in humans shape?

Back 7

1. when the connection bt polypeptides needs to be permanent
2. long strangds or sheets, form strong fibers, act as structure; not water soluble
3. in a ball, water soluble (bc non polar aa are folded toward the inside and the polar onthe outside.) act as enzymes
4. found in skin, hair, nails; alpha helix and twist into fibers; disulfide bridges
5. collagen; triple helix

Front 8

1. Vitamin C is required for
2. what does hemoglobin do? 1 heme can transport how many oxygen molecules?
3. 2 types of protein classification

Back 8

1. (oxidation reaction that adds the OH groups) cross-linking collagen; w/ out it it causes weak skin and joints
2. transport oxygen from lungs throught the blood to all tissues in the body; 4
3. simple and conjugated

Front 9

1. what does it mean when a protein is simple?
2. conjugated?
3. what does it mean when a protein is denatured? what is changed?
4. what happends when globular proteins are denatured? y?

Back 9

1. protein is alone and is able to do its job
2. protein contains other non-protein component called a prosthetic group
3. loss of protein function that results from unfolding of a protein; 2nd, 3rd, 4th
4. lose water solubility(the hydrophobic part that was on the inside is exposed bc its unfolded), form aggregates (clumps bc the hydrophobic aa on the surface of the unfolded protein attract each other by hydrophobic attraction)

Front 10

1. when can denaturation occur?
2. proteins that have carbs covalently added
3. glycoproteins that protect the body from foreign molecules and infections, HOw are they special?
4. they specifically bind to target molecules called

Back 10

1. heat, (vibration breaks H bonds) detergents (breaks hydrophobic bonds), alcohols (disrupt H bonding in 2nd and 3rd structure), acids/base (disrupt salt bridge and H bonds, Hg or Pb (combines w/ SH groups)
2. glycoproteins
3. they have 2 sticky ends
4. antigens

Front 11

1. most enzymes are __ protein
2. RNA enzymes are called
3. the most important ribozyme is a celular structure
4. when a protein is complete enzyme
5. enzyme protein

Back 11

1. globular (highly specific)
2. ribozymes
3. ribosomes
4. simple enzyme
5. enzyme contains some non-protein part.

Front 12

1. the protein part is called
2. the non-protein part is called
3. these together is called
4. cofactors are __
5. coenzyme?

Back 12

1. apoenzyme
2. cofactor
3. holoenzyme
4. inorganic ions
5. organic

Front 13

1. what allows for the enzyme to be specific?
2. what is the active site of an enzyme?
3. how does the substrate fit into the active site?
4. y does the enzyme change shape?

Back 13

1. the shape
2. where the reaction occurs
3. by interactions bt substate and aa side chains
4. to force the functional groups together to form a bond or twist and pull a specific covalent bond to force it to break

Front 14

1. whats the difference bt the lock and key model and induced fit?
2. changes in ph can cause what to happen
3. when an enzymatic reaction has reached its maximum rate, we say that the enzyme

Back 14

1. the substrate shape must match the active site shape exacty in lock and key. only part of the substrate fits precisely in the active site but the remaining parts of the substrate are fitted by the enzyme.
2. changes in charge in aa side chain which affects substrate binding and overall shape
3, is saturated w/ substrate

Front 15

1. the number of chemical reactions that one enzyme molecule can catalzye in 1 min
2. the rate of an enxymatic reaction can be decreased by what?
3. what kind of inhibition is it when the inhibitor is binded by non-covalent interactions?
4. binded by covalent?
5. what kind of inhibition is it when the inhibitor binds to the enzyme's active site?

Back 15

1. turnover number (100000)
2. inhibitors
3. reversible
4. irreversible
5. compettive

Front 16

1. which kind of inhibition is it when the inhibitors binds to a site thats not the active site (how does it inactivate the enzyme?)
2. what is an allosteric enzyme? how many binding sites do they have?
3. when the active site is on one protein chain
4. when the regulator site is on another protein chain
5. when the binding of a negative regulator molecule inactivates the enzyme
6. when the binding of a positive regulator molecule activates the enzyme

Back 16

1. non-compettive (changing the shape so the substrate cant enter or blocking the norma shape change of the enzyme
2. enzymes that have a built in regulatory site that is different from its active site; 2 (active and regulatory)
3. catalytic subunit
4. regulatory subunit
5. negative allosterism
6. postive allosterism

Front 17

1. a form of allosteric regulation where an entire metabolic pathways is regulated by a single unit by the regulation of ONLY THE FIRST ENZYME in pathway
2. a series of enzymatic reations arranged to produce one end product
3. the pathway is regulated by what?

Back 17

1. feedback control
2. metabolic pathway
3. the final product of the pathway (which means that excess production of the product will slow down production