Unit 1 test review part 3 Flashcards

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1
Q

What are proteins

A

Contains an amino and carboxyl group with back bones of N-C-C
polymers of 100-300 amino acids long
22 differnt types

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2
Q

List the 3 types of amino acids

A

1) Hydrophobic- nonpolar
2) Hydrophilic- polar
3)electrically charged-hydrophilic

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3
Q

How do you tell is if a aa is polar or non polar

A

it is polar if it has a oduble bond at end or S,O,N

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4
Q

How to tell how many different tripeptidese can be formed from only 2 amino acids

A

you would do 2(aa)^3 because tripeptides=3 that means 8 diferent possibilities

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5
Q

How to tell if aa is polar non polar or electriclly charged

A

Non polar= Non have a double bond, almost all are made of C & H
Polar=Has double bond of O always except cystein
electriclly charged= Usually eneds with carboxyl or amino group (just memorise them)

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6
Q

What determines the sequence of amino acids in protein

A

The DNA transcribed into MRNA

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7
Q

list 5 functions of proteins

A

1) Structural proteins
2)enzymes
3)Pigment
4)Hormones
5) Immunoglobulin.

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8
Q

Structural proteins soluble or insoluble

A

make up body parts insoluble and tough
eg.Keratin, collagen, bones and teeth, myosin, microtubles and filaments

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9
Q

Enzymes soluble or insoluble

A

biological cataylst
soluble
eg.
1)Amylase hydrolysis reaction of polysaccharides into monosaccharides.
2) Pepsin hydrolysis of protein into amino acids
3) Hydrolysis of lipids into glycerol and 3 fatty acids.

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10
Q

Pigament

A

coloured protein
soluble part of strucutral protein
eg.
melanin
cholrophyll
hemoglobin
anthocynin

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11
Q

Hormones

A

regulitory proteins
control metabolic pathways
adrenalin & thyroxine

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12
Q

Immunoglobin

A

antibodies

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13
Q

Primary structure

A

this determines 2 and 3 structures therefore function of the protin

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14
Q

what are Secondary structures caused by

A

H-Bonds between N-H an C=O of different aa’s causing the chain to fold in helix and b pleated sheet

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15
Q

list 3 facts of B-Pleated sheet

A

1)more than one H bond resulting in larger molecules
2)mostly structural proteins
3)insoluble

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16
Q

List 2 fact on helix shape

A

1)mostly continue to fold in globular proteins
2)soluble

17
Q

What are tertiary structures

A

further foldings caused by r-side chains either
-H-bonds between polar groups
-disulfide cross-linkages between neighboring S-H groups
-Hydrophobic interactions of nonpolar groups.

18
Q

Give 2 examples of quaternary structures

A

1)Hemoglobin 4aa chains with an Fe
2)Insulin 2aa chains

19
Q

Denaturations causes

A

-high heat
-high or low pH
-heavy metals
-organic solvents that dissolve non polar groups
-detergents

20
Q

what type of protein structure is structural proteins

A

secondary b -pleated

21
Q

what type of protein structure is lipase or most enzymes

A

teritery

22
Q

what type of protein structure is anthocyanin pigment

A

teritery