Topic 2

Question 1

How are Biomolecules held together?

Answer 1

Different types of chemical bonds

Question 2

Weak bonds have more or less flexibility?

Answer 2

More

Question 3

Polymers such as DNA are held together

Answer 3

covalent bonds

Question 4

What is held together by covalent bonds

Answer 4

Backbone of polymers
Proteins
DNA
RNA
Polysacchardes

Question 5

Non-covalent bonds are

Answer 5

Electrostatic or ionic

Question 6

T or F: Non-covalent bonds break and reform more covalent bonds

Answer 6

True

Question 7

Are covalent or non-covalent bonds stronger

Answer 7

Covalent

Question 8

Hydrogen bonds

Answer 8

Hydrogen bonded to highly electronegative atom (Nitrogen or oxygen)

Question 9

What liquid is good at hydrogen bonding?

Answer 9

Water!

Question 10

What is created when Electrons spend more time around the e neg atom

Answer 10

a partial charge

Question 11

Van der Waals

Answer 11

Pretty weak
Lots of low-energy interactions
Can interact with hydrophobic surfaces
works like a Velcro

Question 12

Water

Answer 12

Partial negative oxygen
Partial positve hydrogen
Works very well as a bond donor and acceptor

Question 13

entropy of water

Answer 13

High due to free rotation

Question 14

How does water interact with ionic solutes (eg NaCl)

Answer 14

Electrostatically

Question 15

water can form a flickering cluster

Answer 15

Flickering clusters can break and reform in a matter of picoseconds

Question 16

What do you need to break down Ice

Answer 16

input of energy

Question 17

Hydrophobic molecules

Answer 17

will arrange themselves in a way to avoid interactions with water
have hydrophilic head group and hydrophobic tail

Question 18

Entropy

Answer 18

Dissaray in the system

Question 19

The greater the disorder the……. the entropy

Answer 19

higher

Question 20

is high entropy good?

Answer 20

yes

Question 21

macromolecules

Answer 21

Nucleic acids, proteins, lipids, polysaccharides

Question 22

Most Versatile macromolecules

Answer 22

Proteins

Question 23

How are amino acid properties determined

Answer 23

properties determined by R group

Question 24

amino acids stereochemistry

Answer 24

L and D isomers

Question 25

amino acid L isomer

Answer 25

only form found in proteins produced by ribosmes

Question 26

Abs config of amino acids

Answer 26

Corn Rule NH3 has higher priority than COO- group (draw) slide 26

Question 27

how are the 20 common amino acids grouped

Answer 27

On the basis of their side chains

Question 28

amino acid grouping

Answer 28

non polar polar acidic basic

Question 29

Peptide bond

Answer 29

very stable amino acids covalently liked vis peptide bonds

Question 30

half life of peptide bonds

Answer 30

7 years 100 peptide bonds, after 7 years 50 would remain

Question 31

Bonds within peptides

Answer 31

Disulfide bonds hydrogen bonds ionic bonds van der Waals and hydrophobic interactions

Question 32

Protein structure types

Answer 32

Primary structure Secondary Structure Tertiary Structure Quaternary

Question 33

Primary structure (proteins)

Answer 33

includes all covalent bonds and is defined by amino acid sequence the sequence is determined by genes linear sequence of amino acids in a protein

Question 34

Secondary structure (proteins)

Answer 34

regular recurring arrangements in space of adjacent amino acids adopted from polypeptide held together by hydrogen bonds between peptide bonds

Question 35

Tertiary structure (proteins)

Answer 35

Spatial relationship among all amino acids in a polypeptide determines the shapes of a single protein (polypeptide) contained both 1 and 2 structures stabilized by weak bonds

Question 36

Quarternary (proteins)

Answer 36

Protein made up of several polypeptide chains

Question 37

What are the terminuses of proteins

Answer 37

N (amino) terminus and C (carboxyl) terminus

Question 38

Polar molecule

Answer 38

two different ends

Question 39

2 structure alpha helix

Answer 39

forms by bonding every 4 atoms

Question 40

2 structure beta sheet

Answer 40

peptide bonds lie flat so that H bonds can occur can form parallel or antiparallel

Question 41

Intramolecular

Answer 41

within a molecule (protein)

Question 42

Intermolecular

Answer 42

between molecules (protein)

Question 43

How are proteins organized

Answer 43

in domains

Question 44

T or F: most protein domains are 50 to 350 amino acids

Answer 44

True

Question 45

what can protein domains fold into

Answer 45

a conformationally stable discrete unit

Question 46

What determines the function of a protein

Answer 46

The structure

Question 47

Non kinase domains

Answer 47

Src: cytosolic kinase VERGFR2: find a molecule that turns the kinase on

Question 48

Src (cytosolic kinase)

Answer 48

how the protein selects a target

Question 49

what do Denaturation and Renaturation determine

Answer 49

how the protein folds determined by primary sequence

Question 50

Denaturation

Answer 50

unfolds protein

Question 51

Renaturation

Answer 51

folds protein

Question 52

What needs to occur so that denatured molecule can fold back

Answer 52

Dialysis

Question 53

Chaperones

Answer 53

Enzyme utilized in cells to encourage the folding of proteins back to native conformation required input of energy

Question 54

Ubiquitin

Answer 54

76 a.a. protein when tagged onto another protein, that protein gets sent for degradation must have 4 ubiquitin tags for degradation to occur