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BIO 141 Exam > Lecture 2 > Flashcards

Lecture 2 Flashcards

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Biology 101 flashcards
1
Q

3 Attributes Necessary For Life

A

Infromation, Replication and Storage(IRS)

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2
Q

Parts of an Amino acids

A

Amino group on one side, carbon in the middle, Carbonyl group on the other side, side chain at the bottom, and H atom at the top

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3
Q

What groups are side chains divided into

A

Polar, Nonpolar, acidic, and basic

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4
Q

What’s another name for a side chain

A

R group

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5
Q

Whats another name for amino acids

A

Residues

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6
Q

How is the solubility of a protein affected by its chemical properties

A

If the amino acid is charged or polar its hydrophilic and dissolves in water, it the amino acid is uncharged and nonppolar its hydrophobic

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7
Q

How to determine if a an amino acid is polar, nonpolar, acidic, or basic.

A
  1. It it is negatively charged, its acidic
  2. If it is positively charged, its basic
  3. It it is a neutral charge and it has an oxygen atom its polar
  4. If it has none of these its nonpolar
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8
Q

Where do you look to determine either something is polar, nonpolar, acidic or baisc

A

Its R group

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9
Q

peptide bonds

A

These are created when bonds form between a carbonyl group of one amino acid, and amino group of another

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10
Q

what does polymerize mean?

A

It means to be created

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11
Q

How does a peptide bond form

A

It forms through a condensation reaction

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12
Q

What is a condensation reaction?

A

water is formed

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13
Q

What is a polymer

A

Its like what the molecules come together to make

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14
Q

what is the polymer of amino acids

A

Protein

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15
Q

how many types of structures are there in proteins and what are they

A

Their are 4 types of structures, and these structures are primary, secondary, and tertiary structure.

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16
Q

Primary structure

A

The sequence of the amino acids

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17
Q

How are the R groups oriented in the primary structure

A

the R groups stick out of the peptide backbone and interact with each other or water.

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18
Q

What is the Directionality of the sequences

A

it has ends with N terminus( free amino group) and C Terminus (free carbonyl group) and it usually written with the N terminus first.

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19
Q

What is the flexibilty of the sequences

A

either terminus can rotate

20
Q

how many amino acid sequences cna be created?

A

Over 10,000 billion sequences

21
Q

How does the shape and sequence of amino acids affect a protein

A

What a protein does it determined by the shape and sequence of proteins and one change can have a vast effect.

22
Q

What is secondary structure

A

The secondary structure is the result of hydrogen bonding and the bonding of one carbonyl group to one of the amino groups

23
Q

What two shapes result from the secondary structure

A

alpha helix, and beta pleated sheet

24
Q

What does a alpha helix look like

A

It looks like a spring

25
Q

What doe a beta pleated sheet look like

A

It looks like two zigzag area’s joined together.

26
Q

What is a tertiary structure

A

It is a structure that develops from the interactions of the side chains causing the peptide backbone to bend and fold, creating important 3 dimensional shapes.

27
Q

How many interactions are there and what are they

A

There are 5 types of interactions, and they are hydrogen bonding, hydrophobic interactions, Van Der wals interaction, Covalent Bond interaction, and Ionic Bond Interaction

28
Q

What is a hydrogen bonding Interaction

A

from between polar side chains and opposite partial charges

29
Q

What is a hydrophobic interaction

A

Water forces between hydrophobic side chains( nonpolar side chains)

30
Q

What is a Van Der Wals interaction?

A

They are weak electrical interactions between side hydrophobic side chains

31
Q

Oligopeptide

A

It is a chain of fewer than 50 aminoacids

32
Q

Polypetide

A

Chains of 50 or more amino acids

33
Q

Covalent bonding Interaction

A

Covalent bonds bonding between sulfhydryl groups ( Disulfide bonds)

34
Q

Ioninc Bonding interaction

A

forms between groups with full and opposing charges

35
Q

What is a Quaternary stucture?

A

Bonding of distinct polypeptides

36
Q

Types of Quaternary Structures:

A

Dimers, Homedimers, Hetrodimers, Tetramer

37
Q

What is a dimer

A

When two polypeptide sub units bond together.

38
Q

What is a homodimer?

A

When the structure consists of two identical subunity

39
Q

What is a heterodimer

A

When the structure’s sub units are not the same

40
Q

What is a Tetramer?

A

when the structure has 4 polypeptide chains

41
Q

What are moleular chaperones

A

Molecules that facilitate folding in proteins, they are sesponsible for blocking inappropritate interactions between unfolded proteins

42
Q

How can folding be described?

A

It is spontaneous, meaning its due to chemical interactions and usually proteins that are folded are more chemically stable than unfolded proteins

43
Q

What is a Denatrued Protein:

A

Unfolded protein

44
Q

is folding always good.

A

Altough folding is spontaenous and unfolded proteins dont work properly, folding can be infectious.

45
Q

What are Prions?

A

Prions are altered form of proteins and they can induce normal protein molecules to change their shape to the altered form.

46
Q

What is Kuru and hwo does it relate with prions and infectious protein folding?

A

Prions that mess up the shape of proteins cause Kuru a disease that was first found in an area where cannibalism is practiced( eating of the brain, which is very high in prions) and these prions cause proteins to have weird shapes(proteins that can make up the nervous system), this results in an attack on a persons nervous system causing them to laugh uncontrollably, have vast emotional mood swings and termors.

BIO 141 Exam (4 decks)

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