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Biochemistry > Proteins > Flashcards

Proteins Flashcards

1
Q

Oligopeptides
Polypeptides
Proteins

A

2-10
11-49
50 or more

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2
Q

Proteins arrangement

A

Head to tail
N terminus to C terminus

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3
Q

Primary structure is….held together by …
The…is …to the protein

A

Number and sequence of a minor acids in the polypeptide chain
Peptide bonds
Sequence of amino acids /specific

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4
Q

Collagen has which structure

A

None, it has a unique structure to it

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5
Q

Native proteins

A

Newly synthesised proteins ready to work after Golgi modification

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6
Q

Do fibrous proteins have a tertiary structure
Examples

A

No
Collagen, elastin, keratin

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7
Q

Many poly peptides n to c
Many n to c and c to n

A

Parallel
Antiparallel

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8
Q

A change in a single amino acid may cause

A

Profound physiological effects

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9
Q

2 main forms of 2ndry structure

A

A - helical>folding on its axis, stabilized with hydrogen bonds
B pleated sheets> extended chain hydrogen bonds

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10
Q

A-helical must have…..only
Has …..only
While b pleated sheets have…..and……and….

A

1 chain
Intra chain bonds
2-5 chains
Inter and intra chain bonds

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11
Q

R groups of amino acids……. In a-helix

A

Project outwards

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12
Q

Other forms of 2ndry structure

A

Loop regions
b bends
Disordered regions

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13
Q

Tertiary and quaternary

A

Folding into 3D shape, globular proteins only, all bonds
If more than 1 polypeptides enter quaternary structure as well

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14
Q

The bonds 6

A

Peptide> condensation between 2 amino acids
Van der waals>weak interactions
Disulfide> proteins with sulfur, 2 cysteine
Hydrogen>polar side group with water or other polar group
Ionic bonds>NH3+ and COO-
Hydrophobic interactions>non polar R groups

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15
Q

Hydrophobic interactions present

A

In the interior side of the protein

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16
Q

Example of a protein with disulfide bonds

A

Insulin

17
Q

Chaperons

A

Group of molecular proteins that ensure efficient protein folding and prevent aggregation.

*With age chaperons decline causing aggregation and alzheimer’s ,parkinsons, and neurodegenerative diseases.

18
Q

Causes of denaturation

A

Physical>heat/mechanical agitation/UV
Chemical>acids/alkalis/salts of heavy metals

19
Q

After denaturation ….remains

A

Primary structure

20
Q

Heat coagulation test

A

Albumin coagulation due to heat that causes disulfide cross linakge

21
Q

Effects of denaturation

A

Loss of structure
Loss of biological activity
Loss of antigenic property
Less soluble
High digestibility
High viscousity

22
Q

Why higher digestiability

A

Due to the projection of peptide bonds which will be digested by proteolytic enzymes

23
Q

Gluten is
Scleroproteins are
Both are…that yield….only

A

Gliadins and glutelins
Supportive proteins as elastin and keratin
Simple proteins
Amino acids

24
Q

Types of complex proteins

A

phosphoproteins>phosphate connected to OH of serine/threonin/tyrosine> casein of milk
Lipoproteins
Metalloproteins
nucleoproteins> basic protein+RNA/DNA» histones
Chromoproteins
Glycoproteins

25
Q

Glycoproteins have less…and more..
2 types
Examples

A

Carb, protein
N linked, O linked
Amide group of asparagine,, hydroxyl group of serine/threonine
Either with carb radical

26
Q

Chromoproteins
Pigmented group either…or…

A

Metallochromoprotein> iron=red/copper= green blue
No metallochromoprotein > flavo proteins(yellow) D and L amino acid oxidases / melanoproteins(brown/black) like melanokeratin

27
Q

Metallo proteins
Heme iron
Non heme iron
Copper
Magnesium
Manganese
Zinc

A

Hemoglobin,myoglobin
Ferritin(iron storage),transferritin(iron movement)
Superoxidase dismutase/ cytochrome oxidase
Kinases
Arginase
Storage form of insulin/ carbonic anhydrase enzyme

28
Q

Lipoproteins

A

With triacylglycerols and or other lipids(phospholipids/ cholesterol)
Movement of lipids in blood

29
Q

Protein degradation

A

Lysosomal>long half life, digest endocytosed proteins
ATP dependent proteosomal degredation>short half life/abnormal>multistep requiring ubiquitin

30
Q

Half life of a protein is determined by

A

R group of amino acids

Biochemistry (11 decks)

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