Proteins Flashcards

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1
Q

What are proteins composed of?

A

Amino acids

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2
Q

How are amino acids composed?

A

An amino group to the left, carbonyl group on the right, with a CH in the middle called the alpha carbon

The only difference is there r group therefore it’s used to identify them

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3
Q

Where does proteins building stem from?

A

Amino acids

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4
Q

What are proteins?

A

These are amino acids joined together by polypeptides

Most diverse and most important molecule in living organisms

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5
Q

What are the functions of proteins?

A

Structural building blocks

Cellular functions (immune defence, cell to cell transport, oxygen transport)

Genetic operations (growth, repair, and protection)

make enzymes
make hormones
build and maintain tissue

In emergency or starvation they can be broken down or used as an energy source

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6
Q

What does the iodized amino acid look like?

A

N+ O-

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7
Q

non polar

A

R group is a hydrocarbon structure

If sulphur or hydrogen is present it is within the group (not at the bottom)

Electrons are shared relatively equally

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8
Q

Polar

A

The R groups contains sulphur, nitrogen, and/or oxygen

These elements have a higher electronegativity and draw electrons to them resulting in a polar molecule
(But no overall charge is present in the r group)

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9
Q

Electrically Charges Acidic

A

lost H+ ions in the solution, therefore R group is left with negatively charged

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10
Q

Basic

A

accept H ions from the solution, therefore R group is left with a positive charge

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11
Q

what is the SNO rule for polarity?

A

if the R group contains a sulphur, nitrogen, or oxygen then it is polar

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12
Q

what makes an amino acids positive or negatively charged?

A

if it loses H+ ions in the solution, then it is negative=acidic

if it gains H+ ions in the solution, then it is positive=basic

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13
Q

what are the eight essential amino acids

A
must be obtained through the diet
Isoleusine
leucine
Lysine
methionine
phenylalanine
threonine
tryptophan
valine
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14
Q

complete protein

A

food that has full set of all 8 essential amino acids

these foods include animal meat such as red meat, pork, and fish

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15
Q

what is an amide linkage?

A

this is a carbon to nitrogen bond

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16
Q

what is the first level of protein folding and what is it known for?

A

this is called primary,

this is a chain of 50 amino acids linked by peptide bonds

the type of amino acids present or the sequence itself, varied from molecule to molecule

amide linkages are formed between an NH2 (amino group) and a COOH (carboxyl group)

17
Q

what is the second level of protein folding and what is it known for?

A

this is called secondary,

coiling stages in two ways, alpha helix, and beta pleated sheets

consists of interactions with the polypeptide backbone

18
Q

alpha helix vs beta sheets

A

alpha helix: two parts of a polypeptide chain are coiled together, hydrogen are always four amide linkages away between the carboxyl group and amino group

two parts of a polypeptide chain lie parallel, Hydrogens (the stabilizer) form between carbonyl and amino groups

19
Q

hydrophobic vs hydrophilic acid chains

A

hydrophobic has carbon rich side chain, doesn’t react well with water

hydrophilic molecules interact well with water

20
Q

what is the third level of protein folding and what is it known for?

A

this is called tertiary,

strong forces of attraction and repulsion between the polypeptide and its environment force it to undergo additional folding (stringy like hair follicles)

Hydrogens bond between the polar side

Ionic bonds between the oppositely charged side (acid/base)

Vander Waals forces between nonpolar side chains

Disulphide bridges between two cysteines (S-S) (strong stabilizers of tertiary structure

Proline Kinks

21
Q

what is a proline kink

A

naturally bends the alpha helix or beta-pleated sheets where needed

22
Q

what is the fourth level of protein folding and what is it known for?

A

this is called quaternary,

two or more polypeptide subunits must come together to form a functional protein

eg fibrous protein found in hair, hemoglobin

23
Q

denaturation

A

a change in the protein structure formation caused by temperature, ionic concentration, Ph, or environmental factors