Biomolecules 1

Question 1

DNA and RNA Composition

Answer 1

Nucleotide chains

Question 2

Components of a nucleotide

Answer 2

Phosphate (negatively charged), 5 Carbon Sugar, Nitrogen Base

Question 3

Genetics Central Dogma

Answer 3

DNA transcripted to mRNA translated to Protein

Question 4

2 Nitrogen Base Types

Answer 4

Pyrimidine (1 ring) + Purine (2 Rings)

Question 5

Pyrimidine def. + examples

Answer 5

1 Ring. Thymine/Uracil and Cytosine

Question 6

Purine def. + examples

Answer 6

2 Rings. Adenine + Guanine

Question 7

Complimentary Pairs

Answer 7

Guanine + cytosine (3 H bonds). Adenine and Thymine (2 H bonds)

Question 8

DNA Bases + Sugar

Answer 8

A,T,C,G and Deoxyribose

Question 9

RNA Bases + Structure

Answer 9

A,U,C,G + Ribose

Question 10

Transcription Steps (DNA to mRNA)

Answer 10

Initiation, Elongation, Termination

Question 11

Transcription Initiation Desc.

Answer 11

RNA polymerase binds DNA + unwinds 17-18 base pair segment

Question 12

Transcription Elongation Desc.

Answer 12

RNA polymerase synthesises mRNA along DNA template until terminator region is reached

Question 13

Transcription Termination Desc.

Answer 13

Terminator sequence causes RNA polymerase to pause and dissociate. RNA peels away + DNA rewinds to double helix

Question 14

DNA Structure

Answer 14

Double Helix, 2 Strands

Question 15

RNA Structure

Answer 15

Single Strand

Question 16

Translation Steps Desc.

Answer 16

mRNA binds to ribosome in cell cytoplasm. tRNA carries anticodon bases complimentary to mRNA’s codons.

Question 17

Polypeptide Formation Phases

Question 18

Building Unit of A Protein

Answer 18

Amino Acid

Question 19

Open Complex Def.

Answer 19

Exposed 17-18 base pair segment

Question 20

3 Components of a Protein

Answer 20

‘R’/’side’ Chain

Question 21

2 Types of Amino Acids (by R groups)

Answer 21

Non-Polar (Hydrophobic) and Polar (Hydrophilic)

Question 22

Non-Polar Amino Acid Types

Answer 22

Aliphatic (chain) and Aromatic (Ring)

Question 23

Polar Amino Acid Types

Answer 23

Neutral, Alkaline (positive) and Acidic (negative)

Question 24

More amino acid varied Characterstics

Answer 24

Small (can pass through kidney), Branched, Sulpher in side chains, located at protein bend, phosphorylated, glycosylated, nitrosylated

Question 25

Phosphorylated Def.

Answer 25

Adding phosphate molecule

Question 26

Glycosylated Def.

Answer 26

Adding sugar molecule

Question 27

Nitrosylated Def.

Answer 27

Adding of nitroxide

Question 28

Primary Structure Desc.

Answer 28

Polypeptide chain. Peptide bonds between carboxyl group (end) of 1 and amino group (start) of other

Question 29

Secondary Structure Desc.

Answer 29

Rearrangement of primary determined by hydrogen bonds. Folding controlled by amino acid sequence

Question 30

2 Examples of Secondary Structure

Answer 30

Alpha Helix and Beta Pleated Sheet

Question 31

Tertiary Structure Desc.

Answer 31

Folding of secondary into globular form. Hydrophobic amino acids on inside and hydrophilic on outside. Stabalised by bonding and interactions between side chains

Question 32

3 Types of Bonds in Tertiary Structure

Answer 32

Disulphide (2 cytosines), Ionic, Hydrogen

Question 33

Interaction in Tertiary Structures

Answer 33

Hydrophobic

Question 34

Quaternary Structure Desc.

Answer 34

Arrangement of more then 1 polypeptide (2+ polypeptide chains, that are the same/different). Held together by non-covalent interactions + interchain disulphide bonds

Question 35

Covalent Bonds in a protein

Answer 35

Peptide + Disulphide

Question 36

Non-Covalent Bonds in a Protein

Answer 36

Hydrogen, Ionic, Hydrophobic Interactions

Question 37

Native Confirmation of Proteins Def.

Answer 37

Functional fully folded protein structure that determines biological function of the protein

Question 38

Potential Biological Functions of Protein

Answer 38

Enzymatic, Protection, Regulation, Signal Transduction, Storage + Transport

Question 39

Post Translational Modifications

Answer 39

Chemical modification of protein after translation by attaching a functional group. Changing protein function