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
What does catalyzed enzymes do to energy/reaction process? (Think of energy graph)
The catalyzed transition state lowers energy, thus making reaction faster.
26
Definition of active site on enzyme
Location where substrates bind
27
Allosteric Binding
If substrate bonds to enzyme somewhere other than active site.
28
What will cause a change in shape of an enzyme?
Allosteric binding
29
6 Types of Enzymes
1. Transferase 2. Ligand 3. Oxidoreductase 4. Isomer are 5. Hydrolase 6. Lyase
30
Vitamins=
Organic co-factors/co-enzymes
31
Minerals
Inorganic cofactors
32
2 main conditions that affect enzymes
PH and temp
33
Michaelis Menton Equation
Vo=(Vmax [s]/km+[s])
34
2 types of enzyme regulators
1. Allosteric activator (Increase activity) 2. Allosteric inhibitor (decrease activity)
35
2 classes of proteins
1. Enzymatic 2. Non-Enzymatic
36
4 types of non-enzymatic proteins
1. Receptors/ion channels 2. Transport 3. Antibodies 4. Motor
37
Receptors and Ion channel of non-enzymatic proteins
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
Transport non-enzymatic proteins
Ex. Hemoglobin. High concentration of ligand=high affinity Low con. Of ligands=low affinity
39
Antibodies of non-enzymatic proteins
Adaptive immune system (find foreign antigens and destroy)
40
Motor non-enzymatic proteins
Ex. Myosin(when contracting muscles), kinesiology (in trace lunar transport), dynein(motility of cilia)
41
Covalent modifications=
Forming or breaking bonds