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BDS1 - Week 1 HB > Intro to Bio-molecules > Flashcards

Intro to Bio-molecules Flashcards

1
Q

define atoms

A

‘incapable of being divided’

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2
Q

define (Bio/macro) Molecules

A

two or more atoms

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3
Q

define cells

A

smallest living units

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4
Q

define tissue

A

similar cells with common function

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5
Q

define organs

A

two or more tissue types

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6
Q

define organ system

A

cooperative group of organs

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7
Q

define ionic bonding

A

The electrostatic attraction between oppositely charged ions e.g. NaCl

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8
Q

define covalent bonds

A

sharing of electrons e.g. CH4

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9
Q

what does equal sharing of electrons give in covalent bonds

A

non polar bond e.g. CH4

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10
Q

what does unequal sharing of electrons give in covalent bonds

A

polar bond e.g. water

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11
Q

describe hydrogen bonds

A

-hydrogen that is covalently attached to an electronegative atom forms attraction with another v electronegative atom
-they are directional bonds so donor hydrogen and acceptor have to be in same plane e.g. DNA nucleotides
-H bonds are important for DNA and 2° protein structure

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12
Q

describe electrostatic forces

A

-oppositely charged groups attract each other
-amino acids can be ionised and can have interactions between them
-weakened by water and salts becasue they are charged so will compete for electrostatic attraction
-charge on amino acids change according to pH
-this force forms between enzymes and substrate

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13
Q

Describe Van der Waals forces

A

-non specific attraction
-transient asymmetry of electron distribution induces the same in other atoms and an attraction occurs bw the two
-Weak but significant when a number can form at close distance

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14
Q

describe the bonds in water

A

-Biologically important- solvent for large array of molecules
-Electrically polar bc +ve H and -ve O
-Hydrogen bonds- highly cohesive
-Weakens electrostatic & hydrogen bonds
-Nonpolar groups/molecules cluster in water – hydrophobic attractions
-Water-free microenvironments needed for polar reactions bc water will interfere w electrostatic and hydrogen bonds

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15
Q

give polymer for fatty acid

A

Diglyceride, Triglyceride

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16
Q

give polymer for monosaccharide

A

Polysaccharide

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17
Q

give polymer for amino acid

A

protein

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18
Q

give polymer for nucleotide

A

nucleic acid (dna, rna)

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19
Q

describe lipids

A

-structurally diverse
-insoluble in water
-do not form large polymers bc no end to end bonding

20
Q

what are the functions of lipids?

A

Cell membranes (phospholipids)
Storing energy
Insulation, protection & absorbing shocks
Controlling cell activity (steroid hormones)

21
Q

what are fatty acids?

A

long chain carbon molecules which can be saturated or unsaturated

22
Q

what is a triglyceride?

A

a neutral fat made up of glycerol (sugar alcohol) and three fatty acids

23
Q

what is a phospholipid?

A

lipids made of glycerol, phosphate and two fatty acids (one FA replaced with phosphate)

24
Q

what is a sterol?

A

Cholesterol, steroid hormones

25
Q

what is the structure of sterol

A

overlapping C-H rings

26
Q

why is sterol considered to be lipids?

A

because they are hydrophobic

27
Q

describe Low density lipoprotein (LDL)

A

Lipoprotein that carries fatty acids & cholesterol around the body
High levels associated with the development of atherosclerosis (thickening or hardening of the arteries)

28
Q

what are carbohydrates?

A

sugars and polymers of sugars

29
Q

what are the functions of carbohydrates?

A

-short term energy source
-make structural materials e.g. cellulose
-act as molecular tags - glycosylation
-contribute to structure of nucleotides

30
Q

structure of carbohydrates and examples

A

Monosaccharides- five or six sided ring e.g. glucose
Disaccharide e.g. sucrose
Polysaccharide e.g. starch

31
Q

what are proteins?

A

Amino acids linked by peptide bonds
Most abundant & diverse bio-molecule in cells

32
Q

what are the functions of proteins?

A

-structure, muscles made of actin and myosin, hair
-cell transport
-contraction
-signalling
-enzymes
-cell attachment

33
Q

Protein structure

A

Polypeptides of Amino acids (20)
Peptide bonds
Complicated structures (Primary, secondary, tertiary, quaternary)

34
Q

describe collagen

A

Most abundant protein in the body
Support for tissues, skin etc.
Dentin & bone are mineralised collagen

35
Q

how does collagen structure relate to function

A

Triple, cross-linked helix

36
Q

describe nucleotides

A

a nitrogenous base, a phosphate group, and a pentose sugar
C, N & O ring with 5 carbon sugar and phosphate

37
Q

what is the function of nucleotides?

A

to store information needed to control and build cells

38
Q

name the two main types of nucleic acids

A

Deoxyribonucleic acid (DNA)
Ribonucleic acid (RNA)
messenger, transfer, ribosomal, viral

39
Q

describe DNA

A

Double helix,
A, G (Purine), T, C (pyrimidines)
Storage of information in the nucleus

40
Q

describe RNA

A

single stranded,
A, G, U, C nucleotides
Made in the nucleus & mRNA transported

41
Q

describe Amelogenesis imperfecta (AI)

A

Amelogenesis = enamel formation
Teeth discoloured and susceptible to cavities & wear
Mutations in several genes including those coding for ameloblastin & enamelin

42
Q

describe ATP

A

Adenosine triphosphate (ATP)
-made up of ribose sugar, adenine base and phosphate chain
-stores energy for catabolic and anabolic reactions

43
Q

describe nadh

A

Nicotinamide adenine dinucleotide (NADH)
Principle e- donor in respiratory chain
Recycled

44
Q

why is RNA easy to degrade?

A

because it is single stranded

45
Q

what are the functions of biomolecules?

A

-molecular switch
-proteins take part in pathways that create a signal
-molecular motors e.g. flagella/cilia
-sources of energy e.g. ATP
-transport e.g. Hb
-information store eg. DNA
-antibodies/enzymes

46
Q

map to memorise

A

BDS1 - Week 1 HB (3 decks)

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