Proteins Flashcards

(17 cards)

1
Q

Functional group of amino acids

A

Carboxylic and amine group
At normal PH of body fluids, these groups are ionised

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2
Q

What are proteins

A

large organic molecules containing carbon, nitrogen, oxygen, hydrogen

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3
Q

What is the R group

A

The side chain of the amino acid that gives the amino acid a distinctive chemical property

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4
Q

Types of proteins

A

Sarah Really Couldn’t Immunise Tommy’s Cat
S = structural
R = regulatory (neurotransmitters ,hormones for growth)
C = contractile (shortening of muscle fibres)
I = immunology
T = transport
C = catalytic

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5
Q

What are the ‘special’ amino acids

A

Glyciene = simplest amino acid with only a H in its side chain
cysteine = Has sulfur in its side group
Tyrosine = has six carbon ring in its side chain
Lysine = seond amino group in its side chain

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6
Q

How do amino acids bond together

A

Peptide bond forms in a condensation reaction between the carbon in the carboxyl group and nitrogen in the amino group

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7
Q

How are different proteins created

A

There are 20 amino acids, the different arrangement of amino acids in a polypeptide chain creates a different protein as different R group at diff position so diff bonding occurs

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8
Q

Primary structure of protein

A

amino acid sequence genetically determined by cell DNA

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9
Q

Secondary structure

A

Polypeptide becomes 2D as hydrogen bonds form between the O from carboxyl group and H from amino group.
Alpha helix = between every 4th amino acid
Beta pleated = between parallel chains

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10
Q

Tertiary structure

A

Each proteins tertiary structure is unique and determines how protein will function
Bonds are from R group interactions

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11
Q

What bonds are in tertiary structure

A

Disulfide (covalent) - between cysteine amino acids
Weak H bonds
Ionic bonds
Hydrophobic interactions

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12
Q

what are hydrophobic interactions

A

amino acids with hydrophobic R group will fold into the central core while amino acids that have hydrophilic R groups will be at the surface.

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13
Q

quaternary structure

A

Forms in proteins that consist of more than one polypeptide
Bonds are similar to the ones that are in tertiary structure

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14
Q

fibrous proteins

A

Insoluble
Made of long chains lined parallel to each other
Structural functions

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15
Q

Globular

A

Spherical and soluble
Metabolic functions

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16
Q

what is denaturisation

A

Environmental changes causes protein to unfold and lose its characteristic shape, however, denaturisation can sometimes be reversed