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Thanatochemistry > Biochemistry, proteins and enzymes > Flashcards

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
Q

In an aerobic environment, caused by enzymes, organic substances are broken down into much simpler forms of matter.

A

Decomposition

26
Q

Self breaking apart, comes from our own cells that break apart tissues.

A

Autolysis

27
Q

Bacteria that rely on dead or decaying matter.

-enzymes

A

Saprophytic

28
Q

True or false

-Biochemistry expands on organic chemistry

A

True

29
Q
  1. Protein
  2. Carbohydrates
  3. Lipids
  4. Nucleotides
A

The four kinds of compounds that are studied in biochemistry

30
Q
  • Carbon, hydrogen, nitrogen, phosphorus, and sulfur
  • ions: Sodium, magnesium, chloride, potassium, calcium
  • Trace elements: manganese, iron, cobalt, copper, zinc (metallic or metal elements)
A

Types of atoms used in biochemical compounds

31
Q

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
A

Water

32
Q

The goal is to stop proteins from breaking down by cross-linking them.

A

Embalmers

33
Q

These are made by joining amino acids together using a special type of covalent bond called peptide bonds.

A

Proteins

34
Q

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

A

The 4 parts of amino acids

35
Q

This part of the amino acid acts as an acid.

A

Carboxyl group

36
Q

This part of the amino acid acts as a base.

A

Amino group

37
Q

When an amino acid oxidizes, this portion becomes negatively charged.

A

The carboxyl group

38
Q

Amino acids are joined ___1___ end to ___2____ end.

A
  1. Amino

2. Carboxyl

39
Q
  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.
A

The 3 nitrogen containing places in a protein that formaldehyde can insert a methylene bridge.

40
Q

Describes the amino acids joined together by peptide bonds. This is a string of amino acids. (polypeptide)

A

Primary structure of proteins

41
Q

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.

A

Secondary structure of proteins

42
Q

Interaction between the pleated sheet and helices occur giving rise to a unique 3-D shape.

A

Tertiary structure of proteins

43
Q

Interaction of polypeptides. The molecular interactions at each level of protein folding give rise to the protein’s shape.

A

Quatenary structure of proteins

44
Q

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.

A

Hemoglobin

45
Q

Green product of the breakdown of hemoglobin.

A

Biliverdin

46
Q

Yellow product of the breakdown of hemoglobin.

A

Bilirubin

47
Q

Break down small peptide chains into amino acids.

-results in carbon dioxide, water, urea, and energy.

A

Proteolytic enzymes

48
Q

Takes up formaldehyde by neutralizing it, which increases the demand for formaldehyde.

A

Urea

49
Q
  1. Hydrolysis
  2. Deamination
  3. Decarboxylation
A

Types of chemical reactions that cause proteins to break down during putrefaction.

50
Q
  1. Deamination

2. Decarboxylation

A

Types of chemical reactions that cause amino acids to break down during putrefaction.

51
Q

Orderly manner of breaking down proteins that you eat. Stomach uses acidic pH and enzymes to break large proteins into smaller polypeptide chains.

A

Digestion

52
Q

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
A

Enzymes in living people

53
Q

Cause decay and putrefaction.

A

Enzymes in deceased people

54
Q

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.

A

How enzymes catalyze chemical reactions.

55
Q

The reactants upon which the enzyme acts.

A

Substrates

Thanatochemistry (12 decks)

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