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MC Biochem 1 > Chpt 2 > Flashcards

Chpt 2 Flashcards

1
Q

Protein

A
  • Linear, unbranched polymer of 50 or more amino acids
  • Amino acids are connected through peptide bonds
  • the linear sequence of amino acids folds into a 3 Dimensional structure
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2
Q

Functions of proteins (7)

A
  1. Enzymatic Catalysis
  2. Transport and storage
  3. Mechanical Support
  4. Coordinate Motion
  5. Generate and transmission of nerve impulses
  6. Control of growth and differentiation
  7. Immune protection
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3
Q

Function of proteins: Enzymatic Catalysis

A
  • most chemical reactions in the cell are carried out by enzymes, which are globular proteins
  • they increase the rate of chemical reactions by reducing the energy of activation
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4
Q

Function of proteins: Transport and storage

A

-small molecules are moved throughout the cell by specific transporters

Ex: hemoglobin transports O2 in the blood

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5
Q

Function of proteins: Mechanical support

A

-the high tensile strength of bone and skin is due to the presence of collagen, a fibrous protein

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6
Q

Function of proteins: Coordinate motion

A
  • muscles are made mostly of proteins
  • contraction of muscles relies on the sliding motion of two types of proteins, actin and myosin.
  • Motion of a flagella and movement of chromosomes in mitosis also relies on proteins
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7
Q

Function of proteins: Generate and transmission of nerve impulses

A

-sending and receiving messages between nerve cells requires receptor proteins that detects the presence of acetylcholine

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8
Q

Function of proteins: Control of growth and differentiation

A

-proteins turn the expression of other proteins on and off by binding to specific sequences on DNA

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9
Q

Function of proteins: Immune protection

A

-antibodies are highly specific proteins that identify and remove foreign substances from the cell

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10
Q

Amino Acid Backbone

A
  • 20 naturally occurring amino acids are incorporated into proteins
  • proteinogenic amino acids

-other amino acids found in the cell

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11
Q

what form of amino acids are found in living systems

A

L amino acids

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12
Q

Glucogenic vs Ketogenic Amino Acids

A

Glucogenic Amino Acids
-Carbon skeleton is converted into intermediate(s) that can be used to synthesize glucose

Ketogenic Amino Acids

  • Carbon skeleton is converted into intermediate(s) (acetyl CoA or Acetoacetyl CoA) that can form ketone bodies or fatty acids
  • Not substrate for glycogenesis
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13
Q

Essential vs Nonessential Amino Acids

A

Nonessential Amino Acids:
-enzymes present for de novo synthesis of these amino acids

Essential Amino Acids- (Human= TV FILM HWK)

  • Organisms lacks enzymes to synthesize the amino acids
  • Must be obtained from diet
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14
Q

Which amino acids are Glucogenic/nonessential

A
  • Alanine (A, Ala)
  • Arginine (R, Arg)
  • Asparagine (N, Asn)
  • Aspartate (D, Asp)
  • Cysteine (C, Cys)
  • Glutamate (E, Glu)
  • Glutamine (Q, Gln)
  • Glycine (G, Gly)
  • Proline (P, Pro)
  • Serine (S, Ser)
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15
Q

Which amino acids are both glucogenic/ketogenic and nonessential

A

-Tyrosine (Y, Tyr)

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16
Q

Which amino acids are ketogenic and nonessential amino acids

A

None

17
Q

Which amino acids are glycogenic and essential

A

Val (and) His Thr(ee) Met(hods)

  • Histidine (H, His)
  • Methionine (M, Met)
  • Threonin (T, Thr)
  • Valine (V, Val)
18
Q

Which amino acids are both glucogenic/ketogenic and essential

A

ile(y) Trp(ped) BOTH Phe(sants)

  • Isoleucine (I, ile)
  • Phenylalanine (F, Phe)
  • Tryptophane (W, Trp)
19
Q

Which amino acids are ketogenic and essential

A

KETONES in Leu of Lys(ine)

  • Leucine (L, Leu)
  • Lysine (K, Lys)
20
Q

Which R groups have dissociable protons?

-undergo change

A 
Ryan Harris, Do You Even Know Connor? (7)
(R) Arginine (12.5)
(H) Histidine (6.0)
(D) Aspartic acid (3.9)
(Y) Tyrosine (10.9)
(E) Glutamic acid (4.3)
(K) Lysine (10.8)
(C) Cysteine (8.3)
21
Q

If pH is above pKa what happens to the R group?

A

the R group will deprotonate

22
Q

if pH is below pKa what happens to the R group?

A

the R group will be protonated

23
Q

Zwitterionic Form

-just looking at amino backbone (Nitro group and Carboxyl group)

A

Neutral Charge

  • Nitro group Protonated
  • Carboxylic acid Oxygen is deprotonated
24
Q

pKa of Terminal alpha carboxyl group

A

3.1

25
Q

pKa of terminal amino group

A

8.0

26
Q

Peptide bonds

A
  • linear and planar
  • uncharged
  • not free to rotate (due to resonance–>double bond like-steric hindrance)
  • Trans configuration-hydrogen of substituted amino group is trans to the oxygen of carbonyl group
27
Q

What is the only Amino acid that is in the cis configuration instead of trans?

A

Proline

28
Q

Cyclic Amino Acids

A

Proline

29
Q

Aliphatic Def

A 
Nonaromatic Hydrocarbon (C and H only)
-nonpolar hydrophobic
30
Q

Aliphatic Amino Acids

A 
Glycine
Alanine
Valine
Leucine
Isoleucine
31
Q

Sulfur containing Amino Acids

A

Cysteine

Methionine

32
Q

Aromatic Amino Acids

A

Phenylalanine
Tryptophane
Tyrosine

33
Q

Hydroxyl Containing Amino Acids

A

Serine

Threonine

34
Q

Acidic Amino Acids

A 
Aspartic Acid (aspartate-deprotonated form)
Glutamic Acid (Glutamate-deprotonated form)
35
Q

Neutral Amide Acids

A

Asparagine

Glutamine

36
Q

what is the pKa of the terminal alpha-carboxyl group

A

3.1

37
Q

what is the pKa of the terminal alpha-amino group

A

8.0

MC Biochem 1 (30 decks)

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