Biochemistry, proteins and enzymes Flashcards

1
Q

The study of chemical compounds produced and used by living organisms.

A

Biochemistry

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2
Q

Stops decomposition

A

Preservation

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3
Q

Stops microorganisms

A

Disinfection

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4
Q

Contain a carboxyl group (COOH) and an amino group (NH), because they contain the functional groups that act as organic acids and organic bases, amino acids act as either. A compound that acts as an acid and a base (buffer).

A

Amphoterism/Amphoteric

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5
Q

Dipolar ion, another name for an amino acid. Positive on one end, negative on the other.

A

Zwitter ion

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6
Q

A covalent bond, formed by removing a hydroxyl group COH from carboxyl hydrogen (H) from the amino group.

A

Peptide bond

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7
Q

Forming of a peptide bond, removal of a molecule of water to link the two subunits together.

A

Dehydration synthesis

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8
Q

Breaking down in the presence of water. Water molecules are inserted in-between peptide bonds and breaks down the compound into individual amino acids.

A

Hydrolysis

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9
Q

The linking of proteins, occurs between the nitrogens in amino acids.

A

Cross-link

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10
Q

Nitrogen is the side chain in this group (not a functional group).
- Hydroxproline, tryptophan, arginine, and histadine

A

Imide group

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11
Q

Caused by hypostasis, is a result of hemoglobin, red blood cells settle at the bottom of blood vessels and in lower parts of the body. Red discoloration.
-Can be cleared with arterial fluid (moves the blood cells around again).

A

Livor mortis/ post mortem lividity

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12
Q

The settling of red blood cells at the bottom of blood vessels and in the lower parts of the body.

A

Hypostasis

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13
Q

Caused by decomposition, blood cells may break down and leak from the capillaries into the tissue, causing a reddish purple stain.
-beliverdin and bilirubin can leak into the tissue as well (broken down from hemoglobin), causing a greenish or yellow stain.

A

Post mortem stain

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14
Q

The breaking down of blood cells.

A

Hemolysis

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15
Q

Altering the shape of protein and altering its ability to function.

  • Inactivates the protein
  • Caused by increased temperature, lower pH, heavy metals, alcohol.
A

Denature

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16
Q

Protein breaking enzymes that break small peptide chains into individual amino acids.

A

Proteolytic

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17
Q

Occurs in an anaerobic environment, caused by enzymes (human and bacterial in nature) includes hydrolysis, deamination, and decarboxylation.

A

Putrefaction

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18
Q

Involves removing the amino group from an amino acid, products are ammonia and a carboxylic acid.

A

Deamination

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19
Q

Removing the carboxyl group of an amino acid, products simultaneously with deamination.

A

Decarboxylation

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20
Q

The protein part of an enzyme.

A

Apoenzyme

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21
Q

An organic component of an enzyme, often an ion such as Ca2+ or Mg2+ (any trace elements).

A

Cofactor

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22
Q

Organic cofactors - vitamins, ATP, NADH, coenzyme A.

A

Coenzyme

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23
Q

Apoenzyme + cofactors (or coenzymes), able to catalyze reactions.

A

Active enzyme

24
Q

Where chemical reactants bind on an enzyme. Orientation of the substance is often aligned by the cofactors.

A

Active site

25
In an aerobic environment, caused by enzymes, organic substances are broken down into much simpler forms of matter.
Decomposition
26
Self breaking apart, comes from our own cells that break apart tissues.
Autolysis
27
Bacteria that rely on dead or decaying matter. | -enzymes
Saprophytic
28
True or false -Biochemistry expands on organic chemistry
True
29
1. Protein 2. Carbohydrates 3. Lipids 4. Nucleotides
The four kinds of compounds that are studied in biochemistry
30
- Carbon, hydrogen, nitrogen, phosphorus, and sulfur - ions: Sodium, magnesium, chloride, potassium, calcium - Trace elements: manganese, iron, cobalt, copper, zinc (metallic or metal elements)
Types of atoms used in biochemical compounds
31
All of biological chemistry happens in a system based with this. - People are 68-70% composed of this - Special properties make this the ideal substance for biological chemistry to occur in. - high specific heat - high heat of vaporization - high heat of fusion
Water
32
The goal is to stop proteins from breaking down by cross-linking them.
Embalmers
33
These are made by joining amino acids together using a special type of covalent bond called peptide bonds.
Proteins
34
A. Alpha carbon - this is the central carbon B. Carboxyl group - carboxylic acid C. Amino group- amine functional group D. Some have side chains - R group
The 4 parts of amino acids
35
This part of the amino acid acts as an acid.
Carboxyl group
36
This part of the amino acid acts as a base.
Amino group
37
When an amino acid oxidizes, this portion becomes negatively charged.
The carboxyl group
38
Amino acids are joined ___1___ end to ___2____ end.
1. Amino | 2. Carboxyl
39
1. Between the nitrogens in the amino acid side chains. 2. Between the nitrogens in the amino group. 3. Between the nitrogens in the peptide bonds.
The 3 nitrogen containing places in a protein that formaldehyde can insert a methylene bridge.
40
Describes the amino acids joined together by peptide bonds. This is a string of amino acids. (polypeptide)
Primary structure of proteins
41
Hydrogen bonds form between the functional groups of amino acids. This is when the primary structure of proteins is folded into helix and pleated sheet shapes.
Secondary structure of proteins
42
Interaction between the pleated sheet and helices occur giving rise to a unique 3-D shape.
Tertiary structure of proteins
43
Interaction of polypeptides. The molecular interactions at each level of protein folding give rise to the protein's shape.
Quatenary structure of proteins
44
Contains 4 polypeptide chains and 4 hemes. Carries oxygen in the blood and are recycled every 120 days.These break down into biliverdin and bilirubin and carbon monoxide.
Hemoglobin
45
Green product of the breakdown of hemoglobin.
Biliverdin
46
Yellow product of the breakdown of hemoglobin.
Bilirubin
47
Break down small peptide chains into amino acids. | -results in carbon dioxide, water, urea, and energy.
Proteolytic enzymes
48
Takes up formaldehyde by neutralizing it, which increases the demand for formaldehyde.
Urea
49
1. Hydrolysis 2. Deamination 3. Decarboxylation
Types of chemical reactions that cause proteins to break down during putrefaction.
50
1. Deamination | 2. Decarboxylation
Types of chemical reactions that cause amino acids to break down during putrefaction.
51
Orderly manner of breaking down proteins that you eat. Stomach uses acidic pH and enzymes to break large proteins into smaller polypeptide chains.
Digestion
52
In living people, these are protein catalysts that enormously speed up reactions. - lower the energy of activation - speed the rate of spontaneous reactions - can be used over and over again - used in digestion
Enzymes in living people
53
Cause decay and putrefaction.
Enzymes in deceased people
54
Lower the activation energy, therefore increases free energy. (do not add or remove energy). Form a noncovalent complex with their substrates called the enzyme substrate complex (ES complex) at the active site. When the EX complex breaks up, it releases product.
How enzymes catalyze chemical reactions.
55
The reactants upon which the enzyme acts.
Substrates