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Biochemistry Flashcards

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1
Q

As the distance between the nucleus and the electron increases, what occurs?

A

The chemical potential energy also increases.

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2
Q

If the bond angle is 109’5 degrees, has 0 non bonding pairs, what shape is the molecule?

A

Tetrahedral

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3
Q

If the bond angle is 107 and has 1 non bonding pair, what shape is the molecule?

A

Pyramidal

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4
Q

If the bond angle is 104 and had two non bonding pairs, what shape is the molecule ?

A

Bent

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5
Q

If the bond angle is 180 degrees and has 3 non bonding pairs, what shape is the molecule ?

A

Linear

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6
Q

What is molecular polarity dependent on?

A

Shape and bond polarity

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7
Q

Are symmetrical shapes polar or non polar ?

A

Non polar

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8
Q

Asymmetrical shapes are polar or non polar ?

A

Polar

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9
Q

Are intermolecular forces stronger than intramolecular forces ?

A

No, intramolecular forces are stronger.

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10
Q

What are the three types of intermolecular forces?

A

London dispersion forces, dipole-dipole forces and hydrogen bonding .

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11
Q

What is the weakest intermolecular force ?

A

London dispersion forces are the weakest.

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12
Q

True or false: London dispersion forces occur between all molecules.

A

True.

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13
Q

Are London forces temporary ?

A

Yes, London forces are temporary as the occur randomly as there are various instances of unequal distribution of electrons around any given nuclei, creating temporary poles.

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14
Q

Are London forces more significant on smaller molecules?

A

No they are not.

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15
Q

What do dipole dipole forces do ?

A

They hold polar molecules together.

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16
Q

A partially positive side attracts the partially negative side of another molecule. Which force is this ?

A

The dipole dipole forces.

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17
Q

Hydrogen bonding only occurs between what molecules ?

A

When H is attracted to either N, O or F.

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18
Q

Water molecules are attracted to each other by was intermolecular force ?

A

Hydrogen bonding

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19
Q

A molecule that fears water is _______.

A

Hydrophobic .

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20
Q

What is the auto ionization of water ?

A

The production of a H3O+ molecule.

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21
Q

Do acids or bases have an increased level of H30 when dissolved in water.

A

Acids.

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22
Q

There is an increased concentration of OH- molecules in what solutions ?

A

Bases.

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23
Q

What is a buffer ?

A

A chemical balancing system that can donate an H+ ion when required and that can remove a them when there are too many in a solution.

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24
Q

What are the four classes of macromolecules?

A

Carbohydrates, fats, proteins and nucleic acids.

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25
The removal of an H+ ion from one subnit and an OH- from another subnit is what process ?
Dehydration Synthesis
26
Dehydration synthesis is anabolic because ...
It absorbs energy and constructs a larger molecule.
27
The breaking of a macromolecule into their subnits through digestion is what process ?
Hydrolysis.
28
In hydrolysis, what is used to break the covalent bond?
A water molecule.
29
Why is hydrolysis a catabolic reaction?
Due to the releasing of energy through the breaking down of macromolecules.
30
What are the three types of carbohydrates?
Monosaccrides, oligosacchrides, and polysaccharides.
31
Monosacchrides are _______ or _______ .
Aldehydes or ketones.
32
A single carbon chain depicts what type of carbohydrate?
A Monosaccharide.
33
Define Glycosidic linkages.
Covalent bonds that are responsible for holding monosaccharides to one another that are formed by condensation reactions.
34
What process must occur to create a oligosaccharide?
Dehydration synthesis.
35
Maltose is composed of what and is held together by what linkage?
Glucose and glucose, 1-4 linkage
36
What is sucrose composed of and what type of linkage holds it together?
Glucose and fructose, 1-2 linkage.
37
What molecule is composed of glucose and galactose and is held together by a 1-2 linkage?
Sucrose
38
A complex carbohydrate is what type of carbohydrate?
A Polysaccharide.
39
What are the two main purposes of polysaccharides?
Structural support and energy support.
40
Cellulose and chitin serve what purpose?
Structural support.
41
Glycogen and starch serve what purpose?
Energy storage.
42
What happens to excess glucose ?
Enzymes in the chloroplast bind excess glucose together to create starch.
43
What is the main differences between amylose an amylopectin?
Amylose is in branches where as amylopectin branches at 1-6 linkages.
44
Glycogen had a 1-4 glycosidic linkage, and branches of with 1-6 linkages, however, glycogen has several more branches than amylopectin allowing it to...
Hydrolyze at a much faster rate, thus allowing a greater release of energy.
45
Humans store what in their muscles for quick release of energy ?
Glycogen
46
Cellulose differs from starch in what ways ?
It has beta glycosidic linkages and is this used for support instead of energy.
47
What are lipids composed of ?
Carbon, hydrogen and oxygen.
48
Tryglycerols are composed of what ?
3 fatty acids attached to one glycerol.
49
A fat with only single bonds having the max number of hydrogen atoms is what type ?
A saturated fat.
50
An unsaturated fat has what characteristics?
There is atleast one double bond, meaning it does not carry its max number of hydrogen atoms.
51
A polyunsaturated fat differs from an unsaturated fat I'm what way?
Containing multiple double bonds.
52
Functional molecules are what type of macromolecule ?
A protein.
53
What is a biological catalyst?
An enzyme.
54
Define conformation:
Final 3D shape of a protein after sequencing the poly peptide.
55
How many amino acids are considered necessary?
20 amino acids.
56
How many amino acids are considered essential?
8 amino acids.
57
The amide linkage that holds together amino acids in polypeptides are considered what?
Peptide bonds.
58
The sequence of amino acids in a polypeptide strand is what structure ?
The primary structure.
59
Hydrogen bonding causes could and folds the polypeptide strand is what structure?
The secondary structure.
60
An Alpha helix is ...
A tight coil formed by h bonds.
61
How are beta pleated sheets formed?
They are formed between parallel stretches of a polypeptide.
62
What is the tertiary structure of a protein?
The supercoiling of a poly peptide by side gain interactions.
63
What is a disulfide bridge?
Covalent bond between cystein residues in a polypeptide that stabilizes tertiary structure.
64
Quaternary structure involves ...
Two or more poly peptide subnits coming together to form a fictional protein.
65
When can a protein be denatured ?
In high temp and pH changes.
66
What does DNA do ?
It instructs the creation of an organism.
67
What bases does DNA contain ?
A, T, C &G
68
What bases does RNA contain ?
A, U, C & G
69
What does RNA do?
It reads and transports the protein building apparatus to the cell.
70
ATP is responsible for what ?
It drives all energy requiring processes in the body.
71
Chemical Reactants < end products
Endergonic reaction.
72
Exergonic reaction means that ...
The products have less chemical potential energy than the reactants.
73
Define phosphorylation:
The process of attaching a phosphate group to an organic molecule, this rendering it more reactive.
74
What is a redox reaction?
A chemical reaction involving the transfer of one or more electrons from one atom to another where oxidization and reduction occur.
75
Oxidization occurs to the ...
Reducing agent.
76
The oxidizing agent...
Reduces the substance.
77
What speeds up a reaction by lowering activation energy?
An enzyme.
78
A substrate is what ?
The reactant that the enzyme acts upon.
79
What is the site where the enzyme binds to?
The active site.
80
The induced for model states that ..
The protein molecule will change it's shape so that it better fits the enzyme.
81
Competitive inhibitors:
Substance that competes with the enzyme for a substrates binding site.
82
Non competitive inhibitors:
A substance that binds to a binding site that is located away from the active site, causing the change in shape of the enzyme and loss of affinity for its substrate.
83
Define Allosteric Site:
A receptor site that is away from the active site that binds to substrates that allow for inhibition or stimulation of an enzyme.
84
What is feedback inhibition?
A method of metabolic control I'm which a product that has been formed later in the process of a sequence of reactions allosterically inhibits an enzyme that catalyze a a reaction early in the sequence.

Biology (6 decks)

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