Carbon, carbs, lipids and proteins WK 1 Flashcards

1
Q

What are the 4 categories of carbon compounds

A

carbohydrates
lipids
proteins
nucleic acids

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2
Q

Describe carbons structure and binding abilities

A

-four valence e (binds w/other atoms that provide 4 more valence e to fill outer shell)
-carbons bind readily to form long chains, branched molecules/rings (carbon backbone)
-form covalent bonds with H, O, N, S and other

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3
Q

Listen carbons functional groups

A

-hydroxyl (-OH)
-carboxyl (-COOH)
-methyl (-CH3)
-amino (-NH2)
-phosphate (-H2PO4)

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4
Q

Describe carbohydrates and their general formula (providing examples)

A

hydrophilic organic molecules e.g. sugars/starches
-formula: (CH2O)n, n=number of C atoms
e.g. glucose n=6 so formula C6H12O6

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5
Q

Describe the three major monosaccharides and their similarities

A

glucose, galactose, fructose
- formula: C6H12O6 (isomers of each other)
- produced by digestion of complex carbohydrates (starch/disaccharides)
-small intestine/liver convert galactose and fructose=glucose

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6
Q

Define disaccharide. Describe the three important types

A

sugar made of 2 monosaccharides
-sucrose: table sugar (glucose+fructose)
-lactose: sugar in milk (glucose+galactose)
-maltose: grain products (glucose+glucose)

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7
Q

Describe the difference between oligosaccharides and polysaccharides

A

olig.-short chains of 3 or more monosaccharides (at least 10)
poly-long chains of monosaccharides (at least 50)

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8
Q

What are three examples of polysaccharides? Define their functions

A

glycogen: energy storage in cells of liver, muscle, brain, uterus, vagina

starch: energy storage in plants

cellulose - structural molecule in plants important for human dietary fibre

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9
Q

Describe carbohydrates. What occurs when it is digested/oxidised?

A

quickly mobilised source of energy
-when digested=glucose
-oxidised to =ATP

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10
Q

Define conjugated carbohydrates

A

covalently bound to lipid or protein moiety

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11
Q

Define glycolipids, glycoproteins, and proteoglycans

A

Glycolipids: external surface of cell membrane

Glycoproteins: external surface of cell membrane, mucus of respiratory and digestive tracts

Proteoglycans: Gels holding cells and tissue together. Gelatinous filler in eye, joint lubrication and cartilage texture

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12
Q

Define lipids. What are the 5 types in the body

A

-hydrophobic molecules (higher H to O ratio)
-more calories per gram than carbs=better energy storage
types:
fatty acids, triglycerides, phospholipids, eicosanoids, steroids

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13
Q

Describe and define fatty acids. What are it’s types

A

chains of 4-24 C atoms with end carboxyl (-cooh) group
-essential fatty acids obtained from food
-saturated: no double cov bonds
-unsaturated: 1/+ double cov bonds
-polyunsaturated: multiple double

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14
Q

Describe triglycerides and structure

A

store energy, insulate, an act as shock absorption
-3 fatty acids linked to glycerol
-bonds formed by dehydration synthesis
-hydrolysis break down

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15
Q

Describe phospholipids. What is meant by amphipathic

A

similar to neutral fats but one fatty acid replaced by phosphate group (PO4)
amphipathic:
-hydrophobic fatty acid tails
-hydrophilic phosphate head

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16
Q

Describe eicosanoids

A

2- carbon compounds derived from arachidonic acid
-hormone like chemical signals between cells e.g. inflammation, blood clotting

17
Q

Describe steroids

A

lipid with 17 C atoms in four rings
-role in nervous system function and cell membrane structural integrity

18
Q

Describe cholesterol. What is meant by HDL and LDL

A

parent steroid from which others are synthesised

HDL: high density lipoprotein/good cholesterol
lower ratio of lipid to protein-may help prevent cardiovasc. disease

LDL: low density lipoprotein/bad cholesterol
high ratio lipid to protein-contributes to cardiovasc. disease

19
Q

Define protein in terms of amino acids, peptide, peptide bonds

A

polymer of amino acids
a.acid: central C with 3 attachments amino, carboxyl, radical group (determines properties of amino)

peptide: molecule comprising two/more amino acids joined by pep. bond

pep. bond: joins amino acid to carboxyl group of next amino (formed by dehydration synthesis)

20
Q

Describe protein structure (not the 4 types). Define denaturation

A

unique, three dimensional shape crucial to function
-reversibly change conformation therefore function
e.g. muscle contraction

denaturation (extreme conformational change that destroys function)

21
Q

Describe protein primary structure

A

sequence of amino acids encoded in genes

22
Q

Describe protein secondary structure

A

coiled/folded shape held together by H bonds between slightly neg (C=O) and slightly pos (N-H) groups
-alpha helix (spring like) or beta helix (pleated, ribbon like)

23
Q

Describe protein tertiary structure

A

further bending/folding of proteins into globular shapes due to hydrophobic-hydrophilic interactions and Vander Waals force

24
Q

Define globular and fibrous proteins

A

globular: within cell membrane/move freely in body fluids

fibrous: slender filaments suited for roles in muscle contraction and skin/hair strengthening

25
Q

Describe protein quaternary structure

A

associations of two or more polypeptide chains due to ionic bonds and hydrophobic-hydrophilic interactions
-only occurs in some proteins

26
Q

Describe 4 protein functions

A

structure: keratin- tough structural protein of nails/skin surface
collagen- deeper layers of skin, bones, cartilage

cell adhesion: protein bind cells together, keeps tissues from falling apart

membrane transport: channel proteins in cell membrane govern passage
e.g. carriers- transport solutes to other side of membrane

recognition: glycoproteins important for immune recognitions (antibodies=proteins)