terms

Question 1

This amino acid has an aromatic ring and is neutral at pH 7 however when it pH 5 it becomes active

Answer 1

His (histidine)

Question 2

This little guy is non-polar and is very flexible because it has no side chain

Answer 2

Gly (glycine)

Question 3

This amino acid is charged and has a carboxylate group on it

Answer 3

Asp (aspartate)

Question 4

this amino acid 3 carbons in its side chained followed by nitrogen

Answer 4

Lys (lysine)

Question 5

This amino acid is able to form disulfide bonds

Answer 5

Cys (cysteine)

Question 6

This amino acid has an aromatic ring with a hydroxyl group on the end

Answer 6

Tyr (tyrosine)

Question 7

This amino has a small side chain, polar and a hydroxyl group on the end

Answer 7

Ser (serine)

Question 8

this amino acid has a cyclic side chain and is very rigid

Answer 8

Pro (proline)

Question 9

The sequence of amino acid side chains is determined by DNA sequence of gene

Answer 9

primary structure

Question 10

This is the hydrogen bonding of the peptide backbone and not directly dependent on sidecahins

Answer 10

secondary structure

Question 11

this is the 3-dimensional packing of a whole protein chain

Answer 11

tertiary structure

Question 12

this is the interaction between global domains such as actin & myosin, collagen, hemoglobin (association between multiple protein molecules)

Answer 12

quaternary structure

Question 13

this is a protein that is more or less spherical in shape and has less surface area to volume ratio

Answer 13

globular domain

Question 14

This is a protein that is very elongated and usually has some structural function

Answer 14

fibrous protein

Question 15

connects i, i+4 amide groups and is has self-contained hydrogen bonding. binds carbon (i) and another carbon 4 away (i+4`)

Answer 15

alpha helix

Question 16

this are things that allows the amino acid to rotate is two different places and they are known as.

Answer 16

phi/psi angles

Question 17

this is important in understanding protein structure and lead to steric hinderance

Answer 17

torsion angles

Question 18

if molecules are brought to close together and want to repel this is known as

Answer 18

steric hindrance

Question 19

_______ can either lead to the polypeptide being in parallel form or antiparraller

Answer 19

beta sheet

Question 20

without the _____ the enzyme may be unable to function like thiamine is a _____ for pyruvate dehydrogenase

Answer 20

cofactor

Question 21

_____ aka iron

Answer 21

heme

Question 22

this protein is composed of two alpha-helices wrapped around each other and they can be help together by disulfide linkages to become long stiff fibers

Answer 22

keratin

Question 23

A _____ ______l is a structural motif in proteins in which 2-7 alpha-helices are coiled together like the strands of a rope

Answer 23

coiled coil

Question 24

this is essentially a triple helix made from gly-pro-(anything else) and results in a very stiff, strong and is non-strecthy. Therefore it is good for bones and tendons

Answer 24

collagen

Question 25

______ is composed of three polypeptides that are interwound such as DNA

Answer 25

triple helix

Question 26

This occurs when molecules are afraid of water and wanter to be in the middle of the protein away from the water

Answer 26

hydrophobic effect

Question 27

When a protein becomes unfolded this is referred to as

Answer 27

denaturation

Question 28

this is a chaperone that helps unfold misfolded proteins

Answer 28

GroEL/GroES

Question 29

sigmoid curve is the hallmark and when one thing binds more things want to bind. For example when people realize alex is taken all of the sudden they want to join

Answer 29

positive cooperativity

Question 30

the binding sites become weaker after the initial thing binds and makes response to changes in substrate concentration more gradual, allowing for a broader dynamic range

Answer 30

negative cooperativity

Question 31

this is an allosteric effector that binds to hemoglobin lower the binding affinity for oxygens and going towards the T state

Answer 31

2,3-BPG

Question 32

This molecule is a competitive inhibitor with oxygen and can be removed from hemoglobin if p___ drops again

Answer 32

carbon monoxide | ____=CO

Question 33

something that fights with the correct molecule to bind in the active site is known as???

Answer 33

competitive inhibitor

Question 34

Something that binds away from the active site and cause the molecule to become less active

Answer 34

allosteric inhibitor

Question 35

Something that binds away from the active site and cause the molecule to become more active

Answer 35

allosteric activator

Question 36

multiple forms of proteins- | multiple form os enzymes

Answer 36

isoform Ex Hb and HbF | isozyme

Question 37

Helix rest in major groove of DNA and protein fold up around the ZN++ ion. Pretty much the smallest protein

Answer 37

zinc finger protein

Question 38

reconition helix nestles into major groove and contacts bases (reads sequence). Stabilization helix sits behind it, and contacts the DNA backbone.

Answer 38

helix-turn-helix proteins

Question 39

????

Answer 39

examples

Question 40

very similar to chymotrypsin, essentially they are divergent

Answer 40

trypsin

Question 41

this is the precursor to trypsin

Answer 41

trypsinogen

Question 42

_____ has ser, asp and his in the active site and responsible for catalysis

Answer 42

chymotrypsin

Question 43

this is the precursor to chymotrypsin

Answer 43

chymotrypsinogen

Question 44

________ is an enzyme whose zymogen (pepsinogen) is released by the chief cells in the stomach and that degrades food proteins into peptides.

Answer 44

pepsin

Question 45

________ is a non-specific protease (a protein-digesting enzyme) initially obtained from Bacillus subtilis

Answer 45

subtilisin

Question 46

_________ is an enzyme produced by cells of the duodenum and involved in human and animal digestion

Answer 46

enteropeptidase

Question 47

The _____ ______ are a family of enzymes that ydrolyzecertain peptide bonds in other proteins.

Answer 47

serine protease

Question 48

A _____ ______ is a group of three amino acids that are found in the active sites of some proteases involved in catalysis

Answer 48

catalytic triad

Question 49

An _____ _____ is a pocket in the structure of an enzyme which stabilizes a deprotonated oxygen or alkoxide, often by placing it close to positively charged residues. In our case it stables the tertiary structure of the serine protease mechanism

Answer 49

oxyanion hole