chapter 3 Flashcards

1
Q

functional groups

A

Small groups of atoms that are attached to larger molecules giving them specific chemical properties

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2
Q

isomers

A

substances with the same molecular or empirical formula but can exist in different forms

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3
Q

structural isomers

A

substances that have the same molecular or empirical formula but have different carbon skeletons

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4
Q

stereoisomers

A

substances with the same molecular or empirical formula and carbon skeleton, but differ in the arrangement of groups

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5
Q

enantiomers

A

stereoisomers that are mirror images to each other

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6
Q

Chiral molecules

A

a substance that has mirror image versions

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7
Q

State the four basic groups in macromolecules

A

carbohydrates
nucleic acids
protein
lipids

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8
Q

polymer

A

A long molecule built by linking together a large amount of small chemical subunits called monomers
- macromolecules are polymers

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9
Q

dehydration reaction or condensation reaction

A

the formation of covalent bonds between monomers but removing a OH- molecule from one and a H+ molecule from another, thus forming a water molecule

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10
Q

hydration reaction

A

the breaking of covalent bonds between monomers by adding a H+ molecule to one and a Oh_ molecule to another,

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11
Q

Carbohydrates

A

compounds containing carbon, hydrogen and oxygen atoms in the molar ratio 1:2:1

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12
Q

What feature of carbohydrates makes them suitable for energy storage?

A

the release of energy when oxidation occurs due to carbon hydrogen bonds

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13
Q

Monosaccharides

A

the most simple form of carbohydrates

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14
Q

what is the most 6-carbon monosaccharide and what is its function?

A

Glucose, it is a storage molecule.

- it exits in two forms alpha and beta glucose.

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15
Q

State glucoses:

  • structural isomer
  • stereoisomer
A

the structural isomer of glucose is fructose

the stereoisomer of glucose is galactose

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16
Q

disaccharide

A

a substance made from linking two monosaccharides together

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17
Q

transport forms

A

disaccharides that act as glucose reservoirs as enzymes cannot break the bonds between the sub- units to make use of the glucose

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18
Q

Name the two sub- units the come together to make the following transport sugars:

  • sucrose
  • lactose
A

sucrose: glucose and fructose
lactose: glucose and galactose

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19
Q

polysaccharides

A

long polymers that are made of monosaccharides joined by dehydration reactions

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20
Q

glycogen

A

a polysaccharide made entirely of alpha glucose, that has storage functions

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21
Q

how do glucose molecules link?

A

carbon 1 of one molecule links with carbon 4 of another

1 to 4 linkages

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22
Q

cellulose

A

polysaccharide entirely made of beta glucose and has structural functions( make tough fibres)

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23
Q

state the two types of nucleic acids

A

DNA

RNA

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24
Q

State the functions of RNA

A
  • carries information
  • responsible for protein synthesis
    it is involved in control of gene expression
25
Q

What are the monomers of nucleic acids?

A

nucleotides

26
Q

State components of Nucleotides

A
  • pentose
  • 5 sugar group ( ribose or deoxyribose)
  • organic nitrogenous base
27
Q

Phosphodiester bonds

A

bonds that form between nucleotides , through dehydration reactions between phosphates and sugars

28
Q

Name the two groups of nitrogenous bases

A
  • purines

- pyrimidines

29
Q

purines

A

large double ring molecules( Adenine and guanine)

30
Q

pyrimidines

A

Single ring molecules ( thymine , uracil, thymine)

31
Q

What is the function of DNA

A

It stores genetic information

32
Q

Chromosomes

A

structures that form in eukaryotes when DNA is complexed with protein

33
Q

Name the different types of RNA and their functions

A
  • mRNA ( carries information)
  • rRNA ( Part of the ribosome)
  • tRNA ( carries amino acids)
34
Q

Give the defining characteristics of RNA

A
  • uses uracil instead of thymine
  • singe stranded
  • has sugar ribose
35
Q

Give the defining characteristics of DNA

A
  • double stranded

- has sugar deoxyribose

36
Q

The basic components of an amino acid

A
  • an amino group
  • carboxyl group
  • a R group
37
Q

Name and describe the five common amino acid groups groups

A
  • non polar ( contain the R groups CH2 and CH3) leucine
  • polar uncharged ( R groups contain OH or oxygen) threonine
  • Charged amino acids ( R groups containing acids or bases that ionise) glutamic acid
  • Aromatic ( R group contains organic carbon ring with alternating single and double bonds)
38
Q

Peptide bonds

A

covalent bond that links two amino acids ( forms between the amino group of of one molecule and the carboxyl group of another molecule)

39
Q

polypeptide

A

long unbranched chains that are made of amino acids joined by peptide bonds

40
Q

Describe the levels of protein structure

A
  • primary structure ( amino acid sequence )
  • secondary structure( coils and sheets)
  • tertiary structure ( three dimensional shape)
  • quaternary structure ( the arrangement of the protein sub- units )
41
Q

Name and describe the two types of secondary structure

A
  • Alpha helix ( coiled into a spiral shape)

- beta helix ( regions of peptide lined next to each other to form a planar structure)

42
Q

what drives a protein to its tertiary structure

A

hydrophobic expulsion of non polar R groups

43
Q

Van der Waal

A

attractive force between non polar interior of proteins

44
Q

Subunits of a protein

A

individual chains formed by the association of polypeptide chains

45
Q

motifs

A

similarities between otherwise dissimilar proteins

46
Q

domains

A

functional units within a larger structure

substructure within the tertiary structure of proteins’

47
Q

chaperone proteins

A

proteins that help other proteins fold properly

48
Q

denaturation

A

process whereby proteins my change structure or unfold due to a change in the environment

49
Q

What factors can lead to denaturation?

A

change in:

  • pH
  • temperature
  • ionic composition of the surrounding solution
50
Q

what is a result of the denaturation of proteins?

A

Denatured proteins are biologically inactive

51
Q

renaturation

A

the spontaneous refolding of portions of a protein due to the reestablishment of the normal environment of a protein

52
Q

Give the defining characteristic of lipids

A

they are insoluble in water

53
Q

triglyceride

A

structure of a fat molecule( three fatty acids each attached to one carbon on a glycerol molecule)

54
Q

saturated

A

having the maximum number of hydrogen atoms , each carbon molecule is bonded to two hydrogen atoms

55
Q

unsaturated

A

when there are double bonds between two or more pairs of successive carbon atoms in fatty acids

56
Q

what makes lipids excellent energy storage molecules

A

the ratio of energy storing C- H bonds is more than twice that of carbohydrates

57
Q

Describe the structure of phospholipids

A
  • glycerol backbone
  • two fatty acids
  • one phosphate group
    (polar head and two long non polar tails)
58
Q

What is within the interior of phospholipid bilayers

A
  • hydrophobic regions
  • non polar regions
  • fatty acid tails