Biochemistry Flashcards

(70 cards)

1
Q

What makes up the Hydroxyl group

A

Carbon and Hydroxide

C-OH

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2
Q

What makes up the carbonyl group (aldehyde)

A

-C-C–O

H

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3
Q

What makes up the carbonyl group (ketones)

A

-C-C–O

C

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4
Q

What makes up the carboxyl group

A

-C-COOH
OR
-C-C–O
OH

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5
Q

Why doesn’t water dissolve non-polar substances?

A

The partial charges of water are attracted to the charges/partial charges of ionic/polar bonds

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6
Q

What is a hydrogen bond?

A

Bond between the partial positive of a hydrogen of one water and a partial negative of an oxygen of another water

One water can H-bond with with 4 other waters

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7
Q

What are some properties because of Hydrogen bonds

A

High boiling point (all h-bonds must be broken)
adhesion (likes to bond to other things)
Cohesion (water likes to bond to itself e.g surface tension)

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8
Q

What are monomers and polymers and how are they connected

A

monomers are small molecules that are chemically joined to form long chains called polymers

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9
Q

Two metabolic processes

A

Catabolism- the breaking down of polymers

Anabolism- building up of polymers

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10
Q

Condensation/Dehydration synthesis

A

Two monomers join to form a polymer with a removal of H20

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11
Q

Hydrolysis

A

When two monomers are broken apart and an H2O is added

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12
Q

Monosaccharide

A

single sugar molecules
polar
hydroxyl group on each carbon except one
carbonyl group on that one carbon

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13
Q

2 types of monosaccharides

A

Aldose- carbonyl group located on the end of the chain (contains aldehyde)
Ketosde- carbonyl group located on a carbon that is not on the end of the chain (contains ketone)

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14
Q

What glucose can humans use

A

Alpha glucose

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15
Q

Disaccharides

A

two monosaccharides joined together by the condensation reaction, important sources of quick energy

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16
Q

Glycosidic linkage

A

The covalent bond formed between two monomers

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17
Q

What are polysaccharides

A

made up of multiple monosaccharides (large complex carbohydrates)

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18
Q

What are four polysaccharides

A

Animal starch-glycogen
Plant starch-amylose
Cellulose
Chitin

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19
Q

What polysaccharides are used for energy

A

Animal and plant starches, they are also digestible

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20
Q

What are the structural polysaccharides

A

Cellulose and chitin

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21
Q

Why is it important to have a high fibre diet

A

We can’t digest fibre so it fills up the large intestine and helps us expel waste regularly, this helps reduce chances of colon cancer

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22
Q

Why can’t animals digest cellulose

A

Because of the bond between the beta glucoses

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23
Q

What are the general characteristics of lipids

A

3 different groups
Not polymers
Groups differ structurally
Non-polar

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24
Q

Three groups of lipids

A

Fats
Phospholipids
Steroids

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25
What are fats made of
Carbon, hydrogen, oxygen
26
Two types of fat
Saturated | Unsaturated
27
Characteristics of saturated fats
``` solid at room temp no double bonds most animal fats straight chain no double bonds ```
28
Characteristics of unsaturated fats
liquid at room temp double bonds most plant oils bent chain
29
Why are fats necessary
source of essential fatty acids needed for hair and skin part of phospholipids in membranes of cells necessary for absorption of vitamins A,D,E,K
30
How are phospholipids different from other lipids
They have a polar and non-polar regions
31
Basic structure
1 molecule of glycerol 2 fatty acids 1 phosphate group
32
Why are they important
Major component if all cell membranes
33
What is the soluble region
polar head- glycerol and phosphate group
34
What is the insoluble region
Two non-polar fatty acid tails
35
What are three functions of proteins
Hold the body together Defensive proteins right of infection Transport nutrients
36
Monomer of proteins
Amino Acid
37
What does the R group determine for amino acids
``` Identity Physical properties (size and shape) Chemical properties (polar, non-polar, acidic, basic) ```
38
Amino acid polymer
Polypeptide chain
39
Condensation reaction of amino acids
two amino acids form covalent bond between amino group and carboxylic group
40
Primary structure of protein
Amino acid monomers joined to form peptide bonds that create a long chain with amino group on one end and carboxylic on the other
41
Secondary structure of protein
the way polypeptide chain is coiled and folded upon itself
42
Two types of secondary structures
Alpha helix-chain coiled, hydrogen bonds between every 4th amino acid Beta pleated sheet-chain folded back with regions of chain parallel to itself
43
Tertiary structure of proteins
Three dimensional structure of a chain, due to interactions between the R groups and the amino acids that make up the protein
44
Forces holding tertiary confirmation
hydrogen bonds ionic bonds hydrophobic interactions Disulfide bonds
45
Denaturation of protein
Loss of native conformation | Unfolding of tertiary and secondary structures
46
What are proteins sensitive to
temperature pH salt concentration solvent
47
Two types of nucleic acids
Deoxyribonucleic | Ribonucleic
48
Monomer of nucleic acids
Nucleotide
49
Basic structure of nucleotide
5 carbon sugar Phosphate group Nitrogen base
50
Two types of nitrogen bases and how are they different
Purines-double ring | Pyrimidines-single ring
51
What are the pyrimidines
Cytosine Thymine Uracil
52
What are the purines
Adenine | Guanine
53
How are ribose and deoxyribose different
In deoxyribose there is a H at carbon 2 and in ribose there is an OH at carbon 2
54
How many hydrogen bonds form between the base pairs
Cytosine and Guanine-3 | Adenine and Thymine-2
55
How are DNA and RNA related
DNA is the molecule of heredity and RNA is required for the information in genes in DNA to be transcribed and translated
56
What are enzymes
They are proteins that act as catalysts, since they do not participate in the chemical reaction they can be used again
57
What is a substrate
Any molecule recognized by an enzyme and binds to it
58
How do enzymes work
Substrate binds to enzyme active site Enzyme catalyzes the reaction Enzyme is ready to catalyze another reaction
59
What is activation energy and how are enzymes related
It is the energy required to start a chemical reaction, enzymes lower activation energy
60
Co-factor
non-protein atom that binds to an enzyme and is necessary for catalytic activity
61
Co-enzyme
Organic molecule that acts as a co-factor
62
Enzyme inhibitors
Foreign agents that affect the enzymes ability to work
63
How do enzyme inhibitors work
They bind to active sites or other critical sites to lower the rate at which an enzyme catalyzes a reaction
64
Allosteric regulators
Molecules in the body that naturally regulate enzyme activity by binding to the allosteric site on the enzyme
65
Nucleus
Control centre of the cell, contains most of the DNA
66
Nuclear envelope
Made of 2 phospholipid bilayers that have nuclear pores that allow transport in and out of the nucleus
67
Nucleolus
Region inside nucleus where ribosomes are assembeled
68
Smooth endoplasmic reticulum
Proteins from R.E.R are turned into enzymes, they then catalyze formation of all lipids
69
Vesicles
Transport proteins contains digestive enzymes store materials
70
Golgi body
Proteins from R.E.R and S.E.R are modifies then shipped to the vesicles