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2ND YEAR 1ST TERM > MT 6310 LECTURE UNIT 2 PROTEINS > Flashcards

MT 6310 LECTURE UNIT 2 PROTEINS Flashcards

1
Q

Proteins that are the chief constituents of skin, bone, hair, and nails

A

Collagen and Keratin

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2
Q

Agents of catalyzing

A

Enzymes

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3
Q

Proteins involved in muscle movement

A

Myosin and Actin

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4
Q

Protein that transports oxygen from the lungs to cells, other
proteins transport molecules across cell membranes.

A

Hemoglobin

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5
Q

Two types of proteins

A

Fibrous & Globular

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6
Q

A compound that contains both an amino group and a carboxyl group

A

Amino Acid

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7
Q

Term used to describe the un-ionized form of an amino acid

A

Zwitterion

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8
Q

TRUE OR FALSE

The most important aspect of the R groups is their polarity.

A

TRUE

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9
Q

TRUE OR FALSE

With the exception of Cysteine, all protein-derived amino acids have at least one stereocenter and are chiral.

A

FALSE (Glycine exists naturally with the D-configuration)

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10
Q

TRUE OR FALSE

The vast majority of alpha amino acids have the D-Configuration at the alpha carbon.

A

FALSE (most have the L-configuration)

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11
Q

TRUE OR FALSE

Each of the amino acids with one stereocenter exists as 2 enantiomers.

A

TRUE

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12
Q

TRUE OR FALSE

For the 19 of 20 amino acids, the alpha amino group is secondary while for proline it is tertiary.

A

FALSE (19 of 20 have a primary alpha amino group, proline has a secondary alpha amino group)

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13
Q

TRUE OR FALSE

Isoleucine (I) and Threonine (T) contain a second stereocenter.

A

TRUE

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14
Q

TRUE OR FALSE

Amino acids are zwitterions not only in the water solution but also in the solid form.

A

TRUE

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15
Q

The addition of ____ to an amino acid to lower its pH to 0.0 donates a proton to the COO- group of the zwitterion turning it into a positive ion.

A

strong acid (such as HCl)

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16
Q

The addition of a strong base such as NaOH to raise its pH to 14, a proton is transferred from the _____ group to the base turning the zwitterion into a _____ ion.

A

NH3+; negative

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17
Q

The pH at which the majority of molecules of a compound in solution have no net charge.

A

Isoelectricpoint, pI

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18
Q

TRUE OR FALSE

The -SH (sylfhydryl) group of cysteine is easily oxidized to an -S-S- (disulfide)

A

TRUE

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19
Q

The three amino acids that possess an aromatic ring

A

Phenylalanine (Phe, F)
Tyrosine (Tyr, Y)
Tryptophan (Trp, W)

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20
Q

Tryptophan is the precursor to what neurotransmitter?

A

Serotonin

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21
Q

The precursors of norepinephrine and epinephrine are?

A

Phenylalanine and Tyrosine

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22
Q

TRUE OR FALSE

The oxidation of Phenylalanine results in a molecule of Tyrosine.

A

TRUE

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23
Q

The peptide bond refers to the amide bond between what two groups of two amino acids?

A

alpha carboxyl group and the alpha amino group

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24
Q

A biological macromolecule containing at least 30-50 amino acids joined by peptide bonds.

A

Protein

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25
Q

In 1902, who proposed that proteins are long chains of amino acids joined by amide bonds.

A

Emil Fischer

26
Q

He discovered that there is about 40% double bond character to the C-N bond and that a peptide bond between two amino acids is planar.

A

Linus Pauling

27
Q

TRUE OR FALSE

Peptides are written from the left to right, beginning with the free -NH3+ group and ending with the free -COO- group.

A

TRUE

28
Q

At what condition will proteins are least soluble in water at their isoelectric points and can be precipitated from a solution?

A

pH = pI

29
Q

TRUE OR FALSE

A dipeptide refers to 2 amino acids and 1 peptide bond

A

TRUE

30
Q

Myoglobin has how many polypeptides?

A

One

31
Q

Hemoglobin carries oxygen with how many polypeptide chains?

A

Four

32
Q

TRUE OR FALSE

Resonance is high proton delocalization.

A

FALSE (it is ELECTRON delocalization)

33
Q

What do you call polypeptides that are more than 3 but less than 10?

A

Oligopeptides

34
Q

In human insulin, what is the 30th amino acid found in the beta chain?

A

Threonine, Thr

35
Q

In the alpha chain of human insulin, what are the amino acids found in positions 8, 9, and 10 in order?

A

Threonine, Serine, Isoleucine

36
Q

A nonapeptide that is an antidiuretic hormone.

A

Vasopressin

37
Q

Nonapeptide that affects the contractions of the uterus during childbirth and the muscles of the breast that aid in the secretion of milk.

A

Oxytocin

38
Q

Vasopressin has what amino acids that make it different from oxytocin?

A

Arginine and Phenylalanine

39
Q

Oxytocin has what amino acids that make it different from Vasopressin?

A

Leucine and Isoleucine

40
Q

TRUE OR FALSE

The primary structure of a protein determines to a large extent the native secondary and tertiary structures.

A

TRUE

41
Q

TRUE OR FALSE

Vasopressin also stimulates uterine contractions however to a much lesser extent.

A

TRUE

42
Q

What are the conditions in which the alpha helix cannot form in the secondary protein structure?

A
  1. ) the presence of proline

2. ) if a chain possesses an ALL POSITIVE/ ALL NEGATIVE/ ALL HYDROPHOBIC amino acid sequence

43
Q

Globular proteins that contain all three kinds of secondary structures in different parts of their molecules (alpha helix, beta pleated sheet, random coil)

A

Motifs

44
Q

TRUE OR FALSE

The secondary structure can define specific patterns in the domain or functional part of the protein.

A

TRUE

45
Q

In an alpha helix structure, where does the side chains point toward to?

A

outward the helix

46
Q

TRUE OR FALSE

The shape of the alpha helix is maintained by numerous intermolecular hydrogen bonds.

A

FALSE (it is held by INTRAmolecular bonds)

47
Q

TRUE OR FALSE

The shape of the beta pleated sheet is maintained by either intramolecular or intermolecular hydrogen bonds

A

TRUE

48
Q

In all secondary structures, the hydrogen bonding is between what groups?

A

-C=O and H-N groups

49
Q

Another repeated pattern classified as a secondary structure that can be seen in collagen

A

Extended Helix/ Triple Helix

50
Q

In the tertiary structure of proteins, in what ways is it stabilized?

A
  1. ) Covalent bonds
  2. ) Hydrogen Bonds
  3. ) Salt Bridges
  4. ) Hydrophobic interactions
  5. ) Metal ion coordination
51
Q

In tertiary structures, what groups interact to form different types of bonds?

A

R-groups (this makes it different from the secondary group because there it is the C=O and N-H group that bonds.)

52
Q

The arrangement o polypeptide chains into a noncovalently bonded aggregation is called

A

Quaternary Structure of proteins

53
Q

In the quaternary structure of proteins, the individual chains are held together by?

A
  1. ) hydrogen bonds
  2. ) salt bridges
  3. ) hydrophobic interactions
54
Q

TRUE OR FALSE

Fetal hemoglobin contains 2 alpha chains and 2 beta chains.

A

FALSE

Fetal hemoglobin contains 2 alpha chains and 2 gamma chains and they have greater affinity for oxygen than adult hemoglobin.

55
Q

The process of destroying the native conformation of a protein by chemical or physical means.

A

Denaturation (some are reversible and others can permanently damage the protein)

56
Q

This denaturing agent can disrupt hydrogen bonding. In globular proteins, it can cause unfolding of polypeptide chains with the result that coagulation and precipitation may take place.

A

Heat

57
Q

This denaturing agent disrupts hydrogen bonding

A

6 M aqueous urea

58
Q

2- Mercaptoethanol cleaves disulfide bonds by reducing -S-S- groups to -SH groups. It acts as what type of denaturing agent?

A

Reducing Agent

59
Q

What type of denaturing agent have transition metal ions that form water-insoluble salts with -SH groups

A

Heavy Metal ions

60
Q

The Denaturing agent that penetrates bacteria and kill them by coagulating their proteins.

A

Alcohols

61
Q

How many amino acids are there in a turn of an alpha helix structure?

A

3.6 amino acids

2ND YEAR 1ST TERM (3 decks)

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