Proteins Flashcards

(36 cards)

0
Q

What does primary structure determine?

A

1 identity of protein
2 molecular structure
3 functions performed
4 molecular binding

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1
Q

Analytic processes used in the laboratory

A

Chromatography
Electrophoresis
Dye binding
Light absorbance

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2
Q

Properties of secondary structure

A

Strength

Flexibility

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3
Q

3 structures of secondary structure

A

a-helix
B-pleated sheet
Bend conformations or turns

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4
Q

It refers to overall shape or conformation of the protein molecule (known as the fold)

A

Tertiary structure

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5
Q

Results from interaction of side chains

A

Tertiary structure

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6
Q

What does tertiary structure determine?

A

Function

Physical and chemical properties of protein

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7
Q

What stabilizes tertiary structure?

A

Hydrophobic effect
Ionic attraction
Hydrogen bonds
Disulfide

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8
Q

Shape from interaction of more than one protein molecule

A

Quaternary structure

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9
Q

Forces that hold together quaternary structure

A

Non-covalent (H bonds, electrostatic interaction)

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10
Q

Lost of the native or naturally occurring folded structure

A

Denaturation

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11
Q

Denaturation can be accomplished by action of

A

Heat
Acid
Alkali
Enzymes

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12
Q

Contain peptide chains composed of only amino acids

A

Simple proteins

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13
Q

Functions of globular proteins

A

Transporters
Enzymes
Messengers

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14
Q

Characteristics of globular proteins

A

Symmetrical and soluble in water

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15
Q

Characteristics of fibrous proteins

A

Asymmetrical
Inert
With hydrophobic R groups

16
Q

Examples of globular protein

A

Albumin
Hemoglobin
Immunoglobulin

17
Q

Examples of fibrous protein

A

Troponin

Collagen

18
Q

What are conjugated proteins?

A

Proteins that consist of a protein and prosthetic group

19
Q

It defines the characteristics of the protein (conjugated protein)

A

Prosthetic group

20
Q

Examples of conjugated proteins

A

Metalloprotein
Lipoprotein
Glycoprotein
Nucleoprotein

21
Q

Examples of metalloproteins

A

Ferritin (iron)
Cerruloplasmin (copper)
Hemoglobin
Flavoprotein

22
Q

Examples of lipoprotein

23
Q

Examples of glycoprotein

A

Haptoglobin

a-antitrypsin

24
Example of nucleoprotein
Chromatin
25
What is the N content of serum proteins?
16%
26
Other term for prealbumin
Transthyretin
27
Characteristics and properties of protein
1 contain nitrogen atoms 2 can be positively or negatively charged 3 isoelectric point: number of positive = number of negative groups 4 (-) : pH>pI solution and (+) : pH
28
Control protein synthesis
Thyroxine GH Insulin Testosterone
29
Control protein catabolism
Glucagon | Cortisol
30
Degrades extracellular and intracellular proteins
Lysosomal pathway
31
Degrades extracellular proteins
Cytosolic pathway
32
Remove nitrogens from AA
Transaminations
33
Products of transamination
Ammonia | Ketoacids
34
Oxidized and converted to glucose or fat
Ketoacids
35
Converted to urea in hepatocytes and excreted in urine
Ammonia