Biochem topics Flashcards

(55 cards)

1
Q

LIFE:

A

A living thing is essentially a “bag of chemicals” (a cell).

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2
Q

CARBON:

A

Carbon has 4 binding sites, meaning it can bond with 4 other elements. If 4 different elements bind to a single carbon atom, they can form different arrangements called isomers.

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3
Q

Isomer:

A

Molecules with the same composition but arranged differently (e.g., D and L forms).

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4
Q

Enzymes:

A

Molecules that perform work in living things, but only work with specific isomers.

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5
Q

HYDROGEN:

A

A key element associated with hydrogen bonds, which influence molecular shape and structure. Hydrogen is abundant in the universe as a gas.

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6
Q

OXYGEN:

A

A highly reactive element that bonds easily, including with other oxygen atoms.

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7
Q

HYDROCARBONS:

A

The simplest molecules, composed of carbon and hydrogen.

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8
Q

ALCOHOLS:

A

Molecules containing a hydroxyl group (-OH). The hydrocarbon part (R) determines the type of alcohol (e.g., ethanol, propanol, butanol).

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9
Q

ALDEHYDES:

A

Molecules with a carbonyl group bonded to a hydrogen. Many sugars, such as glucose, are aldehydes.

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10
Q

KETONES:

A

Molecules with a carbonyl group bonded to two R groups, without a hydrogen.

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11
Q

ESTERS:

A

Molecules formed by reacting an alcohol with an acid. Many food smells come from esters.

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12
Q

ETHERS:

A

Molecules with an oxygen atom bonded to two R groups. Ethers are vital for lipids, which are essential for cells.

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13
Q

CARBOXYLIC ACIDS:

A

Contain a carboxyl group made of a carbonyl and hydroxyl group. These acids are involved in many biological molecules and interactions.

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14
Q

ANHYDRIDES:

A

High-energy molecules like pyrophosphate. The prefix “pyro-“ means fire or energy. ATP is the most important anhydride.

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15
Q

NITROGEN:

A

Found in amino groups (-NH₂), nitrates (NO₃⁻), nitrites (NO₂⁻), and nitrogen gas (N₂), which makes up 80% of the atmosphere.

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16
Q

AMINO ACIDS:

A

The building blocks of proteins, with a carboxyl group, an amino group, and a variable R group. There are about 20 amino acids, and the L-isomers are predominant in living organisms.

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17
Q

SULFUR:

A

Rare in biological molecules but important when present, such as in sulfhydryl groups (-SH). Sulfur is found in amino acids like cysteine and methionine.

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18
Q

PHOSPHORUS:

A

Commonly found as phosphoric acid in DNA, RNA, and phospholipids. It’s a critical component of ATP, which provides energy.

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19
Q

CARBOHYDRATES:
Monosaccharides:

A

The simplest carbohydrates, with 3–7 carbon atoms (e.g., glucose).

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20
Q

Disaccharides:

A

Two monosaccharides joined together (e.g., lactose, sucrose, maltose).

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21
Q

Polysaccharides:

A

Long chains of monosaccharides used in cell walls and energy storage (e.g., starch, pectin, cellulose).

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22
Q

LIPIDS:
Fatty Acids:

A

Hydrocarbon chains with a carboxylic group.

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23
Q

Triglycerides:

A

Composed of glycerol and three fatty acids.

24
Q

Phospholipids:

A

Lipids with hydrophilic heads and hydrophobic tails, forming bilayers in cell membranes.

25
Waxes:
Lipids with very long hydrocarbon chains.
26
NUCLEIC ACIDS:
Found in cells and viruses; include DNA and RNA.
27
Nucleoside:
A molecule made of a pentose sugar and a purine or pyrimidine.
28
Nucleotide:
A nucleoside with an added phosphate group.
29
DEOXYRIBONUCLEIC ACID (DNA): Primary Structure:
The sequence of bases (~1,000 bases make up a gene).
30
Secondary Structure:
Double-stranded, with complementary base pairing (A-T, G-C).
31
Helix:
A double-stranded structure twisted into a helix (beta DNA).
32
Major Groove:
A larger groove where proteins may bind.
33
Minor Groove:
A smaller groove in the helix, also accessible to certain molecules but less commonly targeted than the major groove.
34
Z-DNA:
A zigzag form observed using X-ray diffraction.
35
RIBONUCLEIC ACID (RNA):
The product of transcription from DNA.
36
Primary Structure:
The linear base sequence.
37
Secondary Structure:
The 2D folding of RNA.
38
Tertiary Structure:
The 3D folding of RNA.
39
PROTEINS:
Made of amino acids linked by peptide bonds.
40
PROTEIN STRUCTURE: Primary:
The sequence of amino acids.
41
Secondary:
Folding due to hydrogen bonds.
42
Tertiary:
Complex 3D folding caused by interactions like disulfide bonds.
43
Quaternary:
The combination of multiple polypeptide chains into a functional protein.
44
ENZYMES:
Globular proteins that act as biological catalysts.
45
Active Site:
The specific area where the substrate binds.
46
Cofactors:
Molecules that help enzymes function.
47
Apoenzyme:
The protein part of the enzyme.
48
Holoenzyme:
The enzyme with its cofactor.
49
Classification:
Enzymes are grouped by their functions, including oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases.
50
ENVIRONMENTAL FACTORS:
Enzymes work best at temperatures of 40–50°C and a pH of 7–8. High temperatures or extreme pH can denature enzymes.
51
INHIBITORS: Competitive:
Chemicals that resemble the substrate and bind to the active site. Reversible. BABY EATS CARROTS, M&M COME, BABY EATS M&M. TAKE AWAY M&M, BABY EATS CARROTS
52
Noncompetitive:
Bind to a different site on the enzyme and alter its shape. Reversible. BABY EATS CARROTS, SIBLING COME, POKES BABY. BABY STOP EATING AND STARTS FIGHTING
53
ALLOSTERIC PROTEINS:
Enzymes with additional regulatory sites that can increase or decrease activity.
54
Positive Effector:
Increases enzyme activity.
55
Negative Effector:
Decreases enzyme activity.