biological molecules Flashcards

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1
Q

how do monomers join together ?

A

in a condensation reaction producing water to form larger polymers

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2
Q

how do polymers break to form monomers ?

A

in a hydrolysis reaction removing water to form monomers

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3
Q

what is the process of joining monomers together to make polymers ?

A

addition polymerisation

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4
Q

draw glycerol and what is molecular formula?

A

C3H8O3
See online or lecture slides for this

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5
Q

draw a fatty acid

A

see online or lecture slides for this

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6
Q

draw the reaction for joining of glycerol and 3 fatty acids

A

see online or lecture slides for this

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7
Q

what does it mean if a fatty acid is saturated?

A

no double carbon bonds

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8
Q

what does it mean if a lipid is amphipathic?

A

has regions of non polar and polar areas

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9
Q

give examples of monosaccharides

A

glucose , fructose , galactose

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10
Q

give examples of disaccharides

A

maltose , sucrose , lactose

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11
Q

gibe examples of polysaccharides

A

starch , glycogen, cellulose

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12
Q

what is the functions of carbohydrates?

A

respiration

storage as glycogen

Combination with proteins or lipids (glycoproteins and glycolipids)
* Hormones
* Cell-cell communications

Incorporation into, or synthesis of, other biological molecules
Functions of carbohydrates

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13
Q

describe nucleotides and draw one

A

Each nucleotide consists of a phosphate
group, a pentose sugar, and a
nitrogenous base.

There are five bases, so five possible
conventional nucleotides.

There are only four in DNA and in RNA;
thymine and uracil play equivalent roles
in DNA and RNA respectively.

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14
Q

what is a pyrimidines?

A

has one carbon-nitrogen ring

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15
Q

what is the nucleotide of the bases : adenine , thymine , cytosine , guanine and uracil ?

A

Base Nucleotide
Adenine Adenosine
Guanine Guanosine
Cytosine Cytidine
Thymine Thymidine
Uracil Uridine

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16
Q

what is a purine ?

A

has two carbon-nitrogen ring

17
Q

what is the nucleotide when the bases are pyrimidine or purines ?

A

Adenine (Purine) Adenosine
Guanine (Purine) Guanosine
Cytosine (Pyrimidine) Cytidine
Thymine (Pyrimidine) Thymidine
Uracil (Pyrimidine) Uridine

18
Q

draw an amino acid

A

see lacture slides

19
Q

what bond forms between amino acids to make polymers/ polypeptides ?

A

peptide bond

20
Q

describe the primary structure of a protein?

A

Sequence of amino acids
Require chemical reactions to alter
Held together by covalent (peptide) bonds.

21
Q

descibe the secondary structure of a protein?

A

How the polypeptide folds locally (in a single area of the polypeptide)
* Areas will fold into one or the other
* Held together by hydrogen bonding

Mostly alpha helices or beta-pleated sheets

22
Q

describe the tertiarty structure of a protein?

A

How the entire polypeptide folds up
* The 3D shape of the polypeptide
* Held together by hydrogen bonds, electrostatic forces,
hydrophilic/hydrophobic interactions, and covalent bonds (disulphide
bridges).

  • Disulphide bridges consist of covalent bonds between sulphur atoms on
    amino acid R groups.
  • Can be (partially) broken by heat
    Protein: Tertiary Structure
23
Q

descibe haemoglobin

A

Haemoglobin
One protein with:
* Four polypeptides
* Two α subunits
* Two β subunits
* Four haem groups

24
Q

describe quaternary structure of protein?

A

number of polypeptides
prosthetic groups

25
Q

describe denaturing

A
  • Proteins are mostly held in a shape by intermolecular forces
  • Attractions and repulsions within the molecule and with the surroundings
  • Heat and pH can break these bonds, causing the folded structure of the protein
    to unravel (denature)
  • The shape of a protein is often directly related to its function. It can not work
    when denatured.
  • E.g. enzymes: If an enzyme changes shape, its active site is no longer
    complementary to its substrate
    Denaturation