Biochemistry Flashcards

(53 cards)

1
Q

4 elements of protein structure

A

Primary- linear amino acid sequence
Secondary- alpha helices and beta-pleated sheets
Tertiary- Folding protein into 3 dimensional shape
Quaternary- multisubunit protein complex

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2
Q

Enzymes are characterized by

A

Specificity, high rate of activity, affinity for their specific substrate (Km), and the maximal rate of reaction when substrate is present in excess concentration (Vmax)

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3
Q

Coenzymes

A

Most vitamins and certain metals act as coenzymes that facilitate enzyme catalytic activity

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4
Q

Carbohydrates are stored as

A

glycogen in the liver and muscle

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5
Q

DNA and RNA 3 main components

A

Purine or pyrimidine base molecule, sugar, phosphoric acid molecule

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6
Q

Protein synthesis occurs

A

on the ribosome where mRNA carries the message and directs the order of AA in the protein, tRNA delivers each amino acid per code, and rRNA catalyzes the assembly of amino acids into protein

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7
Q

4 major biomolecules

A

carbohydrates, amino acids, fatty acids, nucleotides

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8
Q

Biomolecules are building blocks for

A

polysaccharides, lipids, proteins, and polynucleotides

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9
Q

Proteins

A

Form the structural backbone of cells and tissues and are responsible for enzymatic reactions, membrane transport, hormonal regulation, immune system, and transmission of cell to cell messages

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10
Q

All amino acids contain

A

An amino group and a carboxylic acid group and fall into 2 large groupings (primary and secondary amines)

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11
Q

Primary amine

A

nitrogen atom has only one bond to the carbon

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12
Q

Secondary amine

A

Nitrogen atom is bonded to two carbon atoms

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13
Q

Basic amino acids

A

Lysine, arginine, and histidine

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14
Q

Acidic amino acids

A

Glutamate and aspartate

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15
Q

9 essential amino acids

A

histine, leucine, isoleucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine

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16
Q

AA of the urea cycle

A

Urea cycle- conversion of ammonia to urea

arginine, ornithine, and citrulline

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17
Q

Urea cycle

A

Conversion of ammonia to urea
Main pathway for excretion of nitrogen waste product from protein metabolism. Coordinated in the cytoplasm and mitochondria of the cell.

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18
Q

Peptide bond

A

formed between two AA and is the primary element of peptide and protein structure.
Formed in the ribosome
In bond formation direction, loses water, in bond hydrolysis direction gains water

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19
Q

Sickle cell anemia

A

SNP replacing glutamic acid with valine

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20
Q

No post-translational modification of which AA have been identified?

A

Ala, Gly, Ile, or Val

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21
Q

Composition of carbohydrates

A

Carbon, hydrogen, and oxygen

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22
Q

During fasting, glycogen can be

A

hydrolyzed to release glucose and maintain blood sugar levels

23
Q

ABO human blood types

A

Specific glycosylation of cell surface proteins (glycoproteins) as well as the same specific glycosylation of membrane lipids is the base of human blood groups.

24
Q

Lipids include

A

fatty acids, cholesterol, essential vitamins, and glycerides

25
Long chain fatty acids/ phospholipids are precursors for
prostaglandins and leukotrienes
26
Difference between a nucleoside and a nucleotide
Nucleoside- deoxyribose and nitrogenous base pair (AT or CG) | Nucleotide- one to three phosphate groups are added
27
Exons
Sections of DNA that carry specific genes
28
Introns
Sections of DNA that carry no genetic information
29
Enzymes
Basically catalysts, assist in chemical reactions but are not consumed in the reaction. Accelerate the chemistry of getting from a substrate to a product. Accomplish this by lowering the activation energy.
30
Key elements of enzyme-assisted reactions
Specificity- only one or a limited number of closely related substrates Acceleration- Reaction occurs manifold over what would normally occur
31
Stearic or induced fit
The active site of an enzyme is spatially configured to accept only one substrate configuration or a very limited number. This model involves molecular size, orientation or reactive groups, ionic and hydrogen bonding, and possibly movement of the enzyme protein backbone. This model has replaced the original lock and key model of enzyme activity.
32
How do enzymes accomplish their goals? Many explanations exist, but they fall into the following basic categories:
Stearic or induced fit Localized chemistry Transition state
33
An enzyme without its cofactor is an
Apoenzyme or apoprotein
34
Niacin
Can be converted into 2 coenzymes- NAD and NADP
35
Cofactors
Coenzymes that are metals
36
Fat soluble vitamins
A, D, E, K
37
Deficiency associated with Vitamin A
Night blindness
38
Deficiency associated with vitamin D
Rickets
39
Deficiency associated with B2 or B3
Pellagra
40
Deficiency associated with B1/thiamine
Beriberi
41
First order reaction
Substrate goes to product without interaction of another molecule, except the enzyme V=ds/dt=ks
42
Glycolysis
Carbohydrate metabolism | 30-32 moles ATP per mole of glucose
43
Gluconeogenesis
Glucose can be synthesized from noncarbohydrate precursors predominantly in the liver
44
Precursor molecules to glucose
Lactate, pyruvate, glycerol, and keto-acids
45
Ketone bodies
Acetoacetate, beta-hydroxybutyrate, and acetone Concentrations can rise in ketosis or ketoacidosis Brain and heart use ketone bodies as a direct energy source through reconversion to acetyl-coa
46
Propionyl vs acetyl-CoA
If the original fatty acid molecule contains an even number of carbons, then acetyl-CoA is the only product. If the fatty acid chain contains an odd number of carbons, then the terminal product is propionyl-CoA.
47
Cause of DNA damage, missing base
Removal or purine nucleotides by heat or acid
48
Cause of DNA damage, altered base
Alkylating agents, ionizing radiation
49
Cause of DNA damage, wrong base
Deamination
50
Cause of DNA damage, deletion or insertion
Intercalating chemicals
51
Cause of DNA damage, cyclobutyl dimer
UV irradiation
52
Cause of DNA damage, strand breaks
Ionizing radiation, chemicals
53
Cause of DNA damage, strand-cross linking
Chemicals