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Molecules to Medicine Unit 1 > Proteins! > Flashcards

Proteins! Flashcards

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Organic Chemistry 101 flashcards
1
Q

Each amino acid has a __________, ___________, ___________ and __________ around a central carbon.

A

Amino group, Hydrogen, carboxyl and R-group

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2
Q

The four main function of proteins are:

A
  1. Catalysis 2. Transport 3.. Structure

4. Motion

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3
Q

The amino group on the amino acid carried the __________ charge.

A

Positive

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4
Q

The ____________ group on the on the amino acid carried the negative charge.

A

Carboxyl group

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5
Q

The ___________ gives each amino acid its unique properties

A

Side chain / R-group

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6
Q

Name all the of the non-polar/ aliphatic amino acids in order of increasing hydrophobicity.

A
  1. Glycine
  2. Alanine
  3. Valine
  4. Leucine
  5. Methionine
  6. Isoleucine
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7
Q

Name all the aromatic amino acids in order of increasing hydrophobicity.

A
  1. Tyrosine
  2. Tryptophan
  3. Phenylalanine
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8
Q

Name all the polar and uncharged amino acids.

A

Threonine, Serine, Cysteine, Proline, Asparagine, Glutamine

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9
Q

Name all the polar and charged amino acids

A

Histidine, lysine and arginine

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10
Q

Polar and negatively charged amino acids

A

Aspartate, Glutamate

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11
Q

____________ has the ability to form disulfide bonds, which are important in protein stability and structure.

A

Cysteine

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12
Q

Under oxidation conditions, disulphide bridges are _________ whereas under reduction conditions disulphide bridges are ___________

A

Formed; broken

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13
Q

Human insulin is an example of how disulphide bridges can form _________ and ________ linkages.

A

Inter and intra chain linkages

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14
Q

The post-translational ____________ is rich in collagen, yet without vitamin C, doesn’t occur and a person gets ___________

A

Hydroxyproline; Scurvy

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15
Q

The post-translational ___________ is present in several different proteins involved in blood clotting. The lack of modification can be caused by _________ or ____________

A

Carboxyglutamate; vitamin K deficiency; Warfarin

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16
Q

Post-translational glycosylation aids in _________, _________ and ___________

A

Stability, solubility and cell-signaling

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17
Q

Gleevac is a tyrosine kinase inhibitor which inhibits reversible phosphorylation, leading to anti proliferation and treats ___________

A

Chronic Myelogenous Leukemia

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18
Q

Ubiquitination adds a protein with ubiquitine ligase, which _______________

A

Sends the protein to the proteasome to be degraded.

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19
Q

Proteasome inhibitor Valcade prevents Ubiquitination, which treats___________

A

Multiple Myeloma

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20
Q

The peptide bond between the carbonyl carbon and the first amino acid the the amid nitrogen on the second amino acid has ______________ and cannot be rotated

A

Partial double-bond property

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21
Q

The ________ angle is around the central carbon and amid nitrogen bond

A

Phi

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22
Q

The _________ angle is around the central carbon and the carbonyl carbon bond.

A

Psi

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23
Q

Not all Phi and Psi angles are possible because some rotations are inhibited by ____________

A

Steric crowding

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24
Q

There are proteases that can digest any peptide bond such as _______, ________ or __________

A

Trypsin, Chymotrypsin and Pepsin

25
Q

Many blood clotting factors are proteases that exists in their ________ form until trauma initiated their _________

A

Inactive, Cleavage

26
Q

___________ between the protein backbone amide nitrogen and carbonyl oxygen are the driving force for the formation of protein secondary structures.

A

Hydrogen bonds

27
Q

______ and _____ connect alpha helix or beta sheets to form tertiary structures

A

Turns and Loops

28
Q

In an alpha helix, hydrogen bonds formed between the carbonyl oxygen of the _________ amino acid and the amide nitrogen of the __________ amino acid within the same polypeptide chain.

A

nth. n+4

29
Q

Some amin acids, _______ and _______ have a higher tendency to form form alpha helices.

A

Ala and Leu

30
Q

________ and ________ cannot form secondary structures such as alpha helices

A

Proline and Glycine

31
Q

Hemoglobin is mostly _________

A

alpha helical

32
Q

Fibrous tertiary structures are long, have one kind of secondary structure, ____________ and play a protective or structural role

A

insoluble

33
Q

What is a motif?

A

Arrangement of several secondary structure elements

34
Q

What is a domain?

A

Many proteins are made up of multiple stable globular units called domains with more or less independent functions.

35
Q

The most frequently found amino acids in turns and loops are _______ and __________

A

Glycine and proline

36
Q

What is Kd?

A

The binding strength is represented by the dissociation constant Kd

37
Q

Myglobin stores __________ for metabolism, and buries the ________ and oxygen inside the protein.

A

Oxygen; Heme

38
Q

Myglobin can store oxygen but cannot __________

A

Transport oxygen

39
Q

________ has a similar size and shape to O2, so it can fit into the same binding site

A

CO

40
Q

The relaxed state of hemoglobin is ___________

A

Holding onto Oxygen

41
Q

The tensed state of hemoglobin is _____________

A

Releasing Oxygen

42
Q

Positive cooperativity

A

The first bonding even increases the affinity of the remaining sites

43
Q

Oxygen binds well at a _________ pH such as in the lung

A

Higher

44
Q

Oxygen is releases well as a ___________ pH

A

Lower

45
Q

Crystallography

A

Analysis of X-ray diffraction pattern generated by protein crystals

46
Q

NMR

A

Analysis of magnetic resonance signal generate by high concentration of proteins within a magnetic field

47
Q

What does T (m) measure?

A

The temperature or chemical concentration where 50% of proteins are denatured.

48
Q

The Hsp70/Hsp40 folding chaperones are induced during ____________ and bind to the ___________ region of unfolded protein to prevent aggregation.

A

High temperatures; hydrophobic

49
Q

What does protein disulfide isomerase do?

A

Reduces improper disulfide bonds between free Cysteins and reforms them correctly

50
Q

What does propyl isomerase do?

A

Catalyzes the conversion between trans and cis proline which is required for the proper folding of some proteins

51
Q

Deletion of ________ in Cystic Fibrosis causes protein misfolding.

A

F508

52
Q

Gel filtration chromatography

A

Separates proteins based on their size differences

53
Q

Ion exchange chromatography

A

Separates proteins based on their charge differences

54
Q

Affinity Chromatography

A

Utilizes the ability of proteins to bind to specific ligands

55
Q

Edman degredation deteremines

A

N-terminus sequence of the protein

56
Q

Proteins can be identified on a __________ using protein specific __________

A

Western blot; Protein-specific antibodies

57
Q

A smaller Kd, means __________

A

Better binding affinity

58
Q

__________ is involved in N-glycosylation

A

Asparagine

59
Q

_____________ and ___________ are involved in turns and loops.

A

Proline and Glycine

Molecules to Medicine Unit 1 (10 decks)

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