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BIOL 225 > Topic 2 > Flashcards

Topic 2 Flashcards

1
Q

How are Biomolecules held together?

A

Different types of chemical bonds

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2
Q

Weak bonds have more or less flexibility?

A

More

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3
Q

Polymers such as DNA are held together

A

covalent bonds

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4
Q

What is held together by covalent bonds

A

Backbone of polymers
Proteins
DNA
RNA
Polysacchardes

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5
Q

Non-covalent bonds are

A

Electrostatic or ionic

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6
Q

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

A

True

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7
Q

Are covalent or non-covalent bonds stronger

A

Covalent

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8
Q

Hydrogen bonds

A

Hydrogen bonded to highly electronegative atom (Nitrogen or oxygen)

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9
Q

What liquid is good at hydrogen bonding?

A

Water!

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10
Q

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

A

a partial charge

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11
Q

Van der Waals

A

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

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12
Q

Water

A

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

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13
Q

entropy of water

A

High due to free rotation

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14
Q

How does water interact with ionic solutes (eg NaCl)

A

Electrostatically

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15
Q

water can form a flickering cluster

A

Flickering clusters can break and reform in a matter of picoseconds

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16
Q

What do you need to break down Ice

A

input of energy

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17
Q

Hydrophobic molecules

A

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

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18
Q

Entropy

A

Dissaray in the system

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19
Q

The greater the disorder the……. the entropy

A

higher

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20
Q

is high entropy good?

A

yes

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21
Q

macromolecules

A

Nucleic acids, proteins, lipids, polysaccharides

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22
Q

Most Versatile macromolecules

A

Proteins

23
Q

How are amino acid properties determined

A

properties determined by R group

24
Q

amino acids stereochemistry

A

L and D isomers

25
Q

amino acid L isomer

A

only form found in proteins produced by ribosmes

26
Q

Abs config of amino acids

A

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

27
Q

how are the 20 common amino acids grouped

A

On the basis of their side chains

28
Q

amino acid grouping

A

non polar
polar
acidic
basic

29
Q

Peptide bond

A

very stable
amino acids covalently liked vis peptide bonds

30
Q

half life of peptide bonds

A

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

31
Q

Bonds within peptides

A

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

32
Q

Protein structure types

A

Primary structure
Secondary Structure
Tertiary Structure
Quaternary

33
Q

Primary structure (proteins)

A

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

34
Q

Secondary structure (proteins)

A

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

35
Q

Tertiary structure (proteins)

A

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

36
Q

Quarternary (proteins)

A

Protein made up of several polypeptide chains

37
Q

What are the terminuses of proteins

A

N (amino) terminus and C (carboxyl) terminus

38
Q

Polar molecule

A

two different ends

39
Q

2 structure alpha helix

A

forms by bonding every 4 atoms

40
Q

2 structure beta sheet

A

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

41
Q

Intramolecular

A

within a molecule (protein)

42
Q

Intermolecular

A

between molecules (protein)

43
Q

How are proteins organized

A

in domains

44
Q

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

A

True

45
Q

what can protein domains fold into

A

a conformationally stable discrete unit

46
Q

What determines the function of a protein

A

The structure

47
Q

Non kinase domains

A

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

48
Q

Src (cytosolic kinase)

A

how the protein selects a target

49
Q

what do Denaturation and Renaturation determine

A

how the protein folds
determined by primary sequence

50
Q

Denaturation

A

unfolds protein

51
Q

Renaturation

A

folds protein

52
Q

What needs to occur so that denatured molecule can fold back

A

Dialysis

53
Q

Chaperones

A

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

54
Q

Ubiquitin

A

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

BIOL 225 (2 decks)

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