1 Biological Molecules Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

Basic chemical components that make up all cell structures

A
  • carbohydrates
  • proteins
  • lipids
  • nucleotides
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Monomers

A
  • molecules that are subunits of polymers

- e.g. simple sugars, fatty acids, amino acids, nucleotides

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

Polymers

A
  • molecules that consist of multiple monomers

- e.g. carbohydrates, lipids, proteins, nucleic acids

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

Metabolism

A

-all the enzyme-mediated chemical reactions by which cells acquire and use energy as they build and break down organic molecules

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

Condensation

A
  • the process by which an enzyme builds large molecules from smaller subunits
  • (water forms)
  • aka dehydration reaction
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Hydrolysis

A
  • the process by which an enzyme breaks a molecule into smaller subunits by attaching a hydroxyl to one part and a hydrogen atom to the other
  • (water is used)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Carbohydrates

A
  • function: fuel, building material, energy storage
  • structure: formed from monomers of simple sugars, such as glucose
  • monomers can be linked to form larger carbohydrate polymers, known as polysaccharides/complex carbohydrates
  • formula: (CH2O)n
  • made up of carbon (C), hydrogen (H) and oxygen (O) atoms in the ratio 1:2:1
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Monosaccharides

A
  • simple sugars based around a common formula: 6 carbon, 12 hydrogen, 6 oxygen (C6H12O6)
  • structure: different structures possible
  • hexose monosaccharides: glucose, fructose, galactose
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Glucose

A
  • most important biological sugar
  • Properties: highly soluble
  • Function: provides energy for the brain and half of energy for muscles and tissues
    • glucose is immediate energy (glycogen is reserve energy)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Disaccharides

A
  • two monosaccharides covalently linked via glyosidic bonds
  • always contains glucose
  • e.g. maltose, sucrose, lactose C12H22O11
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Maltose

A
  • glucose + glucose
  • (dimer of glucose)
  • makes up starch
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Lactose

A
  • glucose + galactose
  • milk sugar
  • broken down by lactase (those missing the enzyme are intolerant)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Sucrose

A
  • glucose + fructose

- table sugar

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

Polysaccharides

A
  • polymers of hundreds of simple sugars
  • F: structural roles: chitin, cellulose
  • F: energy storage: starch (plants), glycogen (animals), cellulose (plants)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Starch

A

-storage polymer of 𝛼-glucose in plant cells
-insoluble = no osmotic effect on cells
-large = does not diffuse out of cells
made from amylose:
-1,4 glycosidic bonds
-helix with intermolecular H-bonds = compact
and amylopectin:
-1,4 & 1,6 glycosidic bonds
-branched = many terminal ends for hydrolysis into glucose

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

Glycogen

A

-~ 1 million glucose joined by covalent bonds
-main storage polymer of 𝛼-glucose in animal cells
( but also found in plant cells)
-branches every 5-6 glucose
-1,4 & 1,6 glycosidic bonds
-branched = many terminal ends for hydrolysis
-insoluble = no osmotic effect & does not diffuse
out of cells
-compact

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

Cellulose

A

-polymer of 𝛽-glucose gives rigidity to plant cell walls
(prevents bursting under turgor pressure, holds stem up) -1,4 glycosidic bonds
-straight-chain, unbranched molecule
-alternate glucose molecules are rotated 180°
-H-bond crosslinks between parallel strands form
microfibrils = high tensile strength

18
Q

Lipids

A
  • water insoluble cell component
  • no common structures
  • three key types: fats, phospholipids, steroids
19
Q

Fats

A
  • major energy store in the body
  • glycogen is bulky
  • even more energy dense structure
  • provides insulation
  • fat cells produce molecules from the immune system and hormones (Adipokines)
20
Q

Fatty Acids

A

Saturated:

  • contain only single bonds
  • straight-chain molecules have many contact points
  • higher melting point = solid at room temperature
  • found in animal fats

Unsaturated:

  • contain C=C double bonds
  • ‘Kinked’ molecules have fewer contact points
  • lower melting point = liquid at room temperature
  • found in plant oil

Cis:
-two H atoms are on the same side of the double bond= kink in fatty acid

Trans:
-two H atoms are on opposite sides of the double bond= straight fatty acid

21
Q

Triglycerides (fats)

A
  • molecular building blocks of fats
  • glycerol, 3 fatty acid chains
  • assembly through dehydration reactions
22
Q

Phospholipids

A
  • major component of cell membranes
  • similar to triglycerides/fats but only 2 and not 3 fatty acids attached to glycerol, and have phosphate head
  • can form membranes- phospholipid bilayer (hydrophilic head, hydrophobic tails)
23
Q

Steroids

A
  • important components of cell membranes
    • cholesterol
    • sex hormones
    • synthesized in liver or from diet
24
Q

Proteins

A
  • comprises 10-30% cell mass
  • many different functions
  • all proteins are a long polymer chain of amino acid subunits
  • small molecules, 20 total
  • all 20 have a basic structure of a central carbon atom to which the 4 following are attached:
  • hydrogen atom
  • amino group (-NH2)
  • carboxyl group (-COOH)
  • an “R” group
25
Q

Enzymatic proteins

A
  • Function: Accelerating chemical reactions

- Example: Hydrolysis of bonds in food molecules by digestive enzymes

26
Q

Defensive proteins

A
  • Function: Protection against disease

- Example: Antibodies destroy virus and bacteria

27
Q

Structural proteins

A
  • Function: Support

- Example: Collagen and elastin in connective tissue

28
Q

Storage proteins

A
  • Function: Storage of amino acids

- Example: Ovalbumin, the protein of egg white, as an amino acid source for the developing chicken

29
Q

Contractile and motor proteins

A
  • Function: Movement

- Example: Actin and myosin for muscle contraction

30
Q

Hormonal proteins

A
  • Function: Coordination of an organism’s activities

- Example: Insulin regulates blood sugar concentrations by causing glucose uptake

31
Q

Transport proteins

A
  • Function: Transport of substances

- Example: Haemoglobin transports oxygen

32
Q

Receptor proteins

A
  • Function: Response to chemical stimuli

- Example: Receptors of nerve cell detectssignalling molecules

33
Q

Amino acids subgroups

A

The physical and chemical properties of the side chain determine the functional role in a polypeptide

Positively electrically charge side chains (R, H, K)
Negatively electrically charged side chains (D, E)
Polar uncharged side chains (S, T, N, Q)
Special cases (C, U, G, P)
Hydrophobic side chain (A, I, L, M, F, W, Y, V)
34
Q

Beginnings of a Protein

Four Levels of Structure in Proteins

A

Primary structure (polypeptide formation)
-a linear sequence of amino acids
-determines everything else about the protein’s final shape
Secondary structure
-hydrogen bonds twist the polypeptide into a corkscrew- like alpha helix, coil or sheet
-alpha helix (keratin in hair)
-beta pleated sheet (spider web)
Tertiary structure
-secondary structure folds into a functional shape
Quaternary structure
-in some proteins, two or more polypeptide chains associate and function as one molecule (e.g.haemoglobin)

35
Q

Sickle-Cell disease: the importance of protein folding

A
Primary structure:
Glutamine is replaced with valine
Second and Tertiary structure:
Causes a change in the β haemoglobin subunit
Quaternary structure:
Haemoglobin assembles normally
2 faulty β subunits
Impaired function:
Proteins aggregate into a fibre
Less oxygen can be carried
36
Q

Nucleic Acids

A
  • polymers of nucleotide monomers

- joined by sugar-phosphate bonds (include DNA, RNA, coenzymes, energy carriers, messengers)

37
Q

Nucleotide

A
  • monomer of nucleic acids

- has a five-carbon sugar, a nitrogen-containing base, and phosphate groups

38
Q

ATP

A
  • Adenosine triphosphate (ATP)
  • nucleotide that consists of an adenine base, five-carbon ribose sugar, and three phosphate groups
  • F: energy carrier
39
Q

Hysdrolysis of ATP

A

-used to transport molecules or do mechanical work

40
Q

Genetic material

A

Pyrimidines:
Cytosine (C)
Thymine (T), DNA
Uracil (U), RNA

Purines:
Adenine (A)
Guanine (G)

Sugars:
Deoxyribose (DNA - Deoxyribonucleic acid)
Ribose (RNA - Ribonucleic acid)