Proteins And Enzymes Flashcards

1
Q

Watson-Crick Model

A

Theory of genetic info flows in one direction.

DNA—> RNA—> Protein

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2
Q

Retrovirus and an example

A

RNA—> DNA (reverse transcription)

HIV

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3
Q

Formation of Proteins

A

Link AA—> Peptide bonds—> polypeptides—> fold polypeptides—> proteins

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4
Q

Amino Acid Structure

A
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5
Q

What groups link to form peptide bonds

A

On the AA: Amino group and Carboxylic (group) acid

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6
Q

2 ways of breaking peptide bonds

A
  1. Acid hydrolysis
  2. Protcolysis
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7
Q

What two amino acids are alpha helix breakers?

A

Proline and Glycine

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8
Q

What AA forms disulfide bridge?

A

Cysteine

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9
Q

Definition of Hemoglobin

A

AA that picks up oxygen and transports it to tissues in body.

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10
Q

Definition of Zwitterion

A

When AA has a net charge of zero

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11
Q

3 classifications of AA

A

Charge, H bonding ability, and acidic/basic

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12
Q

4 levels of protein structure

A

Primary (1), Secondary (2), tertiary (3), and 4

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13
Q

Primary protein structure

A

Linear sequence, determined by peptide bonds

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14
Q

Secondary protein structure

A

Determined by H bonds, backbone interaction, parallel and anti parallel

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15
Q

Tertiary Protein Structure

A

Determined by H bonds, hydrophobic, disulfide bridges

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16
Q

4 protein structure

A

Multiple polypeptides

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17
Q

Definition of Conformation of protein structure

A

Proteins folded in 3D structure. ACTIVE site

18
Q

Definition of Denatured Protein

A

Proteins that have unfolded. INACTIVE

19
Q

4 things that cause denatured proteins

A

Temp, pH, chemicals, enzymes

20
Q

Sickle cell anemia

A

Genetic mutation that alters the shape of hemaglobin

21
Q

Definition of gene therapy

A

Changing the shape of the mutated proteins

(Still researching as not sure of exact shape of what the proteins are supposed to be.)

22
Q

Enzyme definition

A

Biological catalyst. Enzymes catalyze chemical reactions that happen inside living things

23
Q

2 things to be a catalyst

A
  1. Must speed up reaction.
  2. Cannot be used up or altered in a permanent way
24
Q

4 ways enzymes speed up reactions

A
  1. Acid/base catalysis
  2. Covalent catalyst
  3. Electrostatic catalyst (DNA replication)
  4. Proximity and orientation
25
Q

What does catalyzed enzymes do to energy/reaction process? (Think of energy graph)

A

The catalyzed transition state lowers energy, thus making reaction faster.

26
Q

Definition of active site on enzyme

A

Location where substrates bind

27
Q

Allosteric Binding

A

If substrate bonds to enzyme somewhere other than active site.

28
Q

What will cause a change in shape of an enzyme?

A

Allosteric binding

29
Q

6 Types of Enzymes

A
  1. Transferase
  2. Ligand
  3. Oxidoreductase
  4. Isomer are
  5. Hydrolase
  6. Lyase
30
Q

Vitamins=

A

Organic co-factors/co-enzymes

31
Q

Minerals

A

Inorganic cofactors

32
Q

2 main conditions that affect enzymes

A

PH and temp

33
Q

Michaelis Menton Equation

A

Vo=(Vmax [s]/km+[s])

34
Q

2 types of enzyme regulators

A
  1. Allosteric activator (Increase activity)
  2. Allosteric inhibitor (decrease activity)
35
Q

2 classes of proteins

A
  1. Enzymatic
  2. Non-Enzymatic
36
Q

4 types of non-enzymatic proteins

A
  1. Receptors/ion channels
  2. Transport
  3. Antibodies
  4. Motor
37
Q

Receptors and Ion channel of non-enzymatic proteins

A

Ion channel will let calcium in through the cell membrane bi-layer. Receptors will let ligands in. Ex. Is insulin receptor and insulin as a ligand.

38
Q

Transport non-enzymatic proteins

A

Ex. Hemoglobin.
High concentration of ligand=high affinity
Low con. Of ligands=low affinity

39
Q

Antibodies of non-enzymatic proteins

A

Adaptive immune system (find foreign antigens and destroy)

40
Q

Motor non-enzymatic proteins

A

Ex. Myosin(when contracting muscles), kinesiology (in trace lunar transport), dynein(motility of cilia)

41
Q

Covalent modifications=

A

Forming or breaking bonds