Biology > Chapter 3 > Flashcards

Chapter 3 Flashcards

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1
Q

Monomer

A

A small molecule ( monomers of each kind of biological molecule have similar chemical structures)

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2
Q

Polymer

A

A large molecule formed by linking many monomers

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3
Q

Macromolecule

A

Many molecules bonded together to form a polymer, proteins, carbohydrates, lipids and nucleic acids are important macromolecules

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4
Q

What are the main macromolecules found in living things

A

Proteins, carbohydrates, lipids, nuclei’s acids

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5
Q

What is the carbon chain called?

A

Skeleton or backbone of an organic molecule - is the framework for positioning functional groups

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6
Q

Functional group

A

A specific combination of bonded atoms within a molecule that snows a characteristic set of physical and chemical properties regardless of the molecules its apart of

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7
Q

The chemical behavior of the macro molecules are dictated by

A

The functional groups

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8
Q

Each functional group has its own

A

Different and specific chemical properties

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9
Q

Functional groups are responsible for interactions

A

Within macro molecule and between a macromolecule and other molecules

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10
Q

The arrangement of a functional group determines

A

the properties of the macromolecule (charge, polarity, solubility)

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11
Q

The # and arrangement of functional group give each macromolecule unique properties suchas,

A

Shape, type and strength of intermolecular interactions, such as types of bonds between them, determines name and class it belongs to

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12
Q

Condensation (dehydration) reactions

A

Energy is used to make covalent bonds between monomers to make a polymer; a water molecule is removed with each covalent bond formed

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13
Q

Polymers are only formed

A

If energy is added to the system; it doesn’t happen spontaneously

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14
Q

Hydrolysis reactions

A

Polymers are broken down into monomers; energy is released and a water molecule is added

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15
Q

Water reacts with

A

Covalent bonds that link polymers together

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16
Q

Proteins

A

Most numerous and versatile of the four biomolecules, vary in size shape and function

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17
Q

Protiens vary in

A

Size, shape therefore in function

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18
Q

Amino acids

A

An organic compound containing both amino groups ( NH 2) and a carbonyl group ( coo H) simultaneously both acids and bases because amino groups accept H ions and carbonyl group releases h ions

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19
Q

Amino acids are linked together by

A

Covalently linked peptide linkages through condensation reactions

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20
Q

R group or side chain

A

Contains the fictional groups

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21
Q

Polypeptide

A

Resulting molecule when multiple amino acids are joined covalently by peptide bonds

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22
Q

Protein - monomer

A

Amino acids

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23
Q

Protein- polymer/types

A

Poly peptides

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24
Q

Proteins - bond type

A

Joined covalently by peptide bonds (peptide linkage)

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25
What is the order of the hierarchy of structure?
Primary, secondary, tertiary, quaternary
26
Primary structure
A chain of amino acids that forms loops, coils ands folded sheets from different bond and attraction between functional groups within the chain. Determines the protein's final shape, they are linked together with peptide bonds (very strong)
27
Secondary structure
The primary structure of a single polypeptide interact with itself to form secondary structure, examples are alpha helix and beta pleated sheets they are made with hydrogen bonds.
28
Tertiary structure
Secondary structure of a single polypeptide interact with each other, these interactions are determined by the functional groups I they are made with hydrogen bonds, disulfide bridges; hydrophobic interactions.
29
Quaternary structure
Forms from the ways in which two or more polypeptide chains bind together and interact
30
What are things that can change the secondary & tertiary structures? Why?
Higher temperature, ph changes, high concentrations of polar molecules, nonpolar substances. This is because they are held together by noncovalent and weaker forces
31
What happens when the shape is changed?
The protein function is altered
32
Denature
Destroy the native state properties of a protein or other biological macromolecules, which changes the molecular shape
33
Proteins bind ? To certain molecules
Noncovalently.
34
What proteins bind to depends on what two things?
Shape, and chemistry of exposed surface groups
35
Chaperone
A protein that guards other proteins by counteracting molecular interaction that threaten their 3D structure
36
What happen when the DNA code has a mistake?
It will Change the order of amino acids, which changes the structure of the protein, which prevents he protein from doing its job
37
What are four main biochemical roles for carbohydrates
1 sources of stored energy (glycogen and starch 2 structural support (cellulose, chitin, peptidoglycan) 3 provides the precursor to make the organic molecule and macromolecules of nearly all living cells 4 used to transport stored energy
38
Monosaccharides
One simple sugar; one monomer
39
Disaccharides
Two simple sugars linked by glycosidic linkage
40
Glycosidic linkage
A covalent bond formed between two monosaccharides by a condensation reaction
41
Polysaccharides
Polymers composed of many monosaccharides
42
Glucose
C6H1206
43
Glucose
Most common monosaccharide,6 carbon structure , essential for form aerobic and anaerobic cellular respiration; vital for homeostasis, broken down to release energy as ATP.
44
Carbohydrates - monomer
Monosaccharias
45
Carbohydrates - polymers
Polysaccharides
46
Carbohydrates - bond type
Glycosidic linkage. (Covalent)
47
Polysaccharides do?
Storage material (starch & glycogen) and building material for protection of cell and organism
48
Lipids are characterized by physical properties
Their solubility. They don't dissolve in water
49
Lipids - monomers
Fatty acids
50
Lipids - types
Fats, phospholipids + steroids
51
Lipids - bond type
Ester linkage
52
Lipids are hydrophobic because
The consits of mostly hydrocarbon regions
53
Fats are not polymers they are
Large molecules assembled from smaller molecules by condensation reactions
54
Two kinds of smaller molecules are
Glycerol and fatty acids
55
Main function of fats
Energy storage
56
Saturated fatty acids
All the bonds between the Carbon atoms in the hydrocarbon chain are single bonds
57
Unsaturated fatty acids
One or more double bonds in the hydrocarbon chain, so not all bonds are saturated with hydrogen atoms
58
What is the physical difference between unsaturated and saturated fatty acids?
Saturated are fairly straight unsaturated have kinks in them
59
What effect does the physical properties of the fatty acids do?
Saturated fats are solid at room temp and plant fats are liquid if not added with hydrogen
60
Phospholipids
Essential for cell because they make up biological membranes which form a boundary between the cell and it's external environment or an organelle and the cytoplasm
61
Phospholipid diversity
Based on difference in the two fatty acids and in the groups attached to the phosphate group around its head.
62
Hydrophobic tails
Point towards the interior of the belayer away from the water
63
Hydrophilic heads
On the outside of the belayer comes in contact with the inside & outside of the cell
64
Steroids - Ask
Carbon skeleton consists of four fused rings, vary in-the particular chemical groups attached to the rings
Biology
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