Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Biology > Unit 1 - Biochemistry > Flashcards

Unit 1 - Biochemistry Flashcards

You may prefer our related Brainscape-certified flashcards:
AP® Biology flashcards Biology 101 flashcards
1
Q

What is an independent variable?

A
  • The condition manipulated by the experimenter
  • Time is a common independent variable
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What is a dependent variable?

A
  • The condition that is affected by the independent variable
  • What is measured/recorded
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is a control variable?

A
  • The conditions kept the same
  • Ex., temperature, group under study
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What formula is used to determine the number of electrons in each shell?

A

2n2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Explain how you can identify protons, neutrons, and electrons in a given element

A
  • Protons: the atomic number
  • Electrons: depends on the charge; neutral = the same number as protons
  • Neutrons: the mass number – the atomic number (or will be indicated)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What are ionic bonds?

A

Chemical bonds that occur between two elements that wish to gain or lose electrons (typically a metal and non-metal) to complete or lose an outer shell.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What are covalent bonds? Polar vs. nonpolar?

A

Chemical bonds that occur between two elements that wish to share electrons (typically a non-metal and non-metal) to feign completion of an outer shell.

Covalent bonds can either be polar (covalent between non-identical elements) or nonpolar (covalent between the same elements).

  • Polar bonds have partial charges, depending on the element that has a stronger attraction for electrons
  • Nonpolar bonds are completely neutral
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What are hydrogen bonds?

A

Hydrogen bonds occur between hydrogen and FONS. These are all partial attractions that are created by polar bonds.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Four Properties of Water

Explain cohesion in water

A

Cohesion

  • Water molecules form hydrogen bonds with one another, resulting in high surface tension
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Four Properties of Water

Explain adhesion in water

A

Adhesion

  • Water molecules form hydrogen bonds with other polar molecules, counters gravity by bonding to cell walls
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What makes water a good temperature moderator?

A

Water as a Temperature Moderator (ie sweating?)

  • Hydrogen bonds can absorb more eat then standard bonds due to their strong intermolecular forces
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Four Properties of Water

What makes water a good solvent?

A

Water as a Solvent

  • Often called the universal solvent, as it is polar and can break up most substances
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What are functional groups?

A

Groups of atoms that determine the characteristics and chemical reactivity of a substance

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What is an isomer?

A

Isomer: two molecules are isomers if they have the same chemical formula (Ex., C2H6O) but different molecular structures.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What do you call a molecule with a single bond? double bond? triple bond?

A

Alkane, alkene, alkyne

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What is a peptide bond? State the formula.

A

A peptide bond is a special type of amide linkage found between 2 amino acids

(O=C-N-H)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What are “linkages”?

A

Functional groups of different molecules frequently interact to form bonds called linkages, which are always found in the middle of molecules.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Describe disulfide linkage

A

A disulfide linkage refers to the linkage formed between 2 thiols when H2 is removed

  • S-S
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Describe amide linkage

A

An amide linkage occurs when the elements of water are removed between an amine and a carboxyl group

  • O=C-N
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Describe an ester linkage

A

An ester linkage occurs when the elements of water are removed between an alcohol and carboxyl group

  • O-C=O
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Describe anhydride linkage

A

An anydrige linkage occurs when the elements of water are removed between 2 carboxyl groups

  • O=C-O-C=O
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Describe an ether linkage

A

An ether linkage occurs when the elements of water are removed between 2 alcohol groups

  • Often found in carbs
  • C – O – C
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Define monomer and give an example

A

Monomer: small building blocks of polymers (ex., glucose, a monomer, makes up glycogen, a polymer)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Define polymer and give an example

A

Polymer: large molecules composed of smaller building blocks (ex., DNA is comprised of nucleotides)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

Define thermodynamics

A

Thermodynamics: the study of energy flow. In biology, this is called bioenergetics

26
Q

Define redox reaction

A

Redox reaction: oxidation and reduction reactions generally occur together, as electrons are highly reactive. As one molecule is oxidized, another is quickly reduced. These are called redox reactions.

27
Q

Living System Reactions

What is condesnation?

A

Condensation occurs when two molecules are joined by a covalent bond by the removal of H2O

  • Sign: H2O is a product, but not the only product
28
Q

Living System Reactions

What is hydrolysis?

A

Hydrolysis occurs when large molecules are split into smaller ones by the addition of H2O

  • Sign: H2O is a reactant with something else and “splits” it to create the products
29
Q

Living System Reactions

What is an exothermic/exergonic reaction?

A

Exothermic reactions occur when energy is released/lost

  • Sign: energy is a product
30
Q

Living System Reactions

What is an endothermic/endergonic reaction?

A

Endothermic reactions occur when energy is gained/absorbed

  • Sign: energy is a reactant
31
Q

Living System Reactions

What is oxidation?

A

Oxidation occurs when any substance is combined with oxygen OR loses an electron

  • Sign: oxygen is a reactant and creates a combined product OR an electron is a product
32
Q

Living System Reactions

What is reduction?

A

Reduction occurs when oxygen is removed in a reaction OR when an electron is gained

  • Sign: oxygen is a product OR an electron is a reactant
33
Q

Living System Reactions

What is neutralisation?

A

Neutralisation occurs when acids and bases react to produce a salt and water. This is called a neutralisation reaction since the solution is no longer acidic or basic

34
Q

State the four biologically important molecules

A

There are four types of these molecules (called macromolecules):

  1. Carbohydrates
  2. Lipids
  3. Proteins
  4. Nucleic Acids
35
Q

What are carbohydrates?

A

Molecules that consist of C:2H:O.

There are 4 subtypes of carbohydrates:

  1. Monosaccharides (single sugars)
  2. Disaccharides (2 single sugars)
  3. Oligosaccharides (3-10 simple sugars)
  4. Polysaccharides (long chains)
36
Q

Explain monosaccharides

A

Monosaccharides (single sugars)

  • Most are classified by the number of carbons they contain (Ex., triose has 3 carbons, tetrose has 4)
  • Exceptions include glucose (major energy supply for plants and animals), fructose, and galactose, which are all isomers of each other
37
Q

Explain disaccharides

A
  • Disaccharides (2 single sugars attached together via a special ether linkage called a glycosidic linkage)*
  • Ex., sucrose (fructose + glucose), lactose (glucose + galactose) and maltose (glucose + glucose)
38
Q

Explain oligosaccharides

A

Oligosaccharides (3-10 simple sugars)

39
Q

Explain polysaccharides

A
  • Polysaccharides (complex carbohydrates consisting of many monomer units forming long chains)*
  • They have two major functions: structural support (ex., cellulose, chitin) and energy storage (ex., starch, glycogen)
40
Q

What are lipids?

A
  • Hydrophobic molecules consisting of C:H:O and ending in OH.
  • They are involved in energy storage, hormones, and cell membranes.

There are 3 subtypes of lipids:

  1. Oils and Fats
  2. Phospholipids
  3. Steroids (Sterols)
41
Q

Explain oils and fats

A

Oils and Fats

  • These are produced by condensation reactions between 1 molecule of glycerol and 3 molecules of fatty acids (long CH hydrocarbon chains) (an ester linkage, ex triglyceride)
  • They are the most common energy-storing molecules in living organisms
42
Q

Explain phospholipids

A
  • Phospholipids*
  • These are mostly found in cell membranes and are composed of 1 glycerol, 2 fatty acids, and 1 polar nitrogen groups. The polar nitrogen head is hydrophilic (loves water) and the nonpolar fatty acids are hydrophobic.
43
Q

Explain steroids

A
  • Steroids (Sterols)*
  • Steroids are composed of 4 fused “rings” with several functional groups and are synthesized from cholesterol. They function as hormones (ex., testosterone)
44
Q

What are proteins?

A
  • Proteins are composed of amino acids and possess two functional groups: amine and carboxyl.
  • Proteins function as enzymes, hormones, hemoglobin, and antibodies.

There are 3-4 steps to the structure of a protein:

  1. Primary
  2. Secondary
  3. Tertiary
  4. Quaternary
45
Q

Explain the steps of the protein structure

A
  • Primary*
  • This refers to the specific sequence of amino acids in the protein
  • Secondary*
  • This refers to the coiling or folding of the amino acid chain
  • Tertiary*
  • This refers to the three-dimensional globular structure (multiple folding)
  • Quaternary*
  • This refers to the interaction of 2 or more tertiary structures (not all proteins have this)
46
Q

What are nucleic acids?

A
  • Nucleic acids are used to store genetic information.
  • They are the only molecules that can produce clones of themselves.
  • Examples include DNA, RNA (helps DNA synthesis proteins), and ATP.
  • Five types of nitrogenous bases are found in nucleic acids: adenine, thymine (not RNA), guanine, cytosine, Uracil (RNA’s thymine replacement) (ring like with lots of N)
47
Q

Define essential amino acids

A

Essential amino acids are amino acids that cannot be made by the body. As a result, they must come from food.

48
Q

What are catalysts?

A
  • A molecule that speeds up the rate of a chemical reactions
  • These are not consumed in the reaction; they are not reactants
  • They function by reducing the required activation energy of a reaction
49
Q

What are enzymes?

A
  • Enzymes are biological catalysts, influenced by temperature, shape, pH
  • They are proteins with complex and changing shapes and:
    • Are highly specific about their substrate
    • Their activity can be regulated (enhanced/supressed)
50
Q

What two ways can a substrate interact with an enzyme?

A

There are two ways the substrate can interact with the enzyme: the lock-and-key model in which the substrate fits perfectly, or the induced-fit model, where the substrate is induced to fit perfectly.

51
Q

What is allosteric control?

A

Enzymes have control sites where a specific substance can bind to and alter the enzyme shape. There are two types of these substances:

  • The activator, which primes the enzyme (turns it “on”)
  • The inhibitor, which distorts the enzyme (turns it “off”)
52
Q

What is end-product inhibition (a.k.a. feedback inhibition)?

A

End-product inhibition occurs when the enzyme is switched off due to an increased concentration of the end product. There are two types of this inhibition:

  1. Competitive inhibition, where an end-product similarly shaped as the enzyme binds at the active site
  2. Non-competitive inhibition, where an end-product binds away from the active site; at the control site. This is an example of allosteric control.
53
Q

Define metabolism

A

Metabolism: any chemical reaction in the body.

54
Q

Define anabolism

A

Anabolism: small molecules building up into larger ones (Ex., amino acid à protein)

55
Q

Define catabolism

A

Catabolism: large molecules breaking down into smaller ones

56
Q

Define ATP

A

ATP: adenosine tri-phosphate - a nucleic acid. When ATP is called upon, it releases one of its 3 phosphates, becoming ADP and releasing energy for the cell. This process can be reversed.

57
Q

Draw an amino acid with peptide bond

A
58
Q

Draw glucose

A
59
Q

Show this reaction: glycerol + fatty acids –> triglyceride

A

ESTER

60
Q

Draw an enzyme control diagram

A

Biology (7 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions