Proteins, Protein Structure, Classification of Proteins (TOPIC 2 PROTEINS) Flashcards

(36 cards)

1
Q

Composition of Proteins

A

Carbon
Hydrogen
Oxygen
Nitrogen

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2
Q

Majority of proteins are synthesized from the?

A

liver and some in plasma cells (immunoglobulins).

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3
Q

The most abundant and important macromolecules in the body.

A

Proteins

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4
Q

can acts as acids or bases depending on the pH (Zwitterion).

A

Amphoteric

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5
Q

Negatively (-) charge at alkaline pH.

A

Amino Group

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6
Q

Positively (+) charge at acidic pH.

A

Carboxylic Group

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7
Q

Transport Proteins

A

Albumin
Hemoglobin
Transferrin
Ceruroplasmin

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8
Q

pressure exerted by proteins in extracellular fluid. Decrease oncotic results to edema.

A

Oncotic pressure regulator (albumin)

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9
Q

Proteins from the food are breakdown into amino acids via

A

Hydrolysis

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10
Q

Protein catabolism (breakdown) is increased by ?

A

Glucocorticoids therapy and thyroid hormones

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11
Q

Protein anabolism (synthesis) is increased by

A

androgens, growth hormones and insulin.

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12
Q

Proteins primarily synthesized in the liver.

A

Alpha, beta globulins, fibrinogen and albumin

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13
Q

Immunoglobulins (antibodies) are synthesized in the

A

RTE system specifically the plasma cells.

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14
Q

REGULATION: Protein level is regulated by ____, ____ of _____ and _____

A

diet, rate of metabolism and hormones.

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15
Q

EXCRETION: Reabsorbed in the kidneys (normal: < _____mg/__H) anabolic (deamination) products are excreted in the urine such as ammonia and urea

A

150
24

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16
Q

Proteins Structures

A

Primary
Secondary
Tertiary
Quaternary

17
Q

Protein structure that refers to the sequence of amino acid in peptide or protein.

A

Primary structure

18
Q

Protein structure that refers to
Local folding of the polypeptide chain into helixes and sheets.

A

Secondary structure

19
Q

Types of Secondary protein structure

A

Alpha helix
Beta sheet
Beta turn

20
Q

3 dimensional folding pattern of protein due to interaction of side chains

A

Tertiary structure

21
Q

Unfolding of this pattern is called

A

DENATURATION.

22
Q

Consist of 2 or more polypeptide chain or sub units forming a larger unit.

Example: hemoglobin (4 subunits)

A

Quaternary structure

23
Q

Consists only of amino acids

A

Simple Protein

24
Q

What are the Simple Proteins

A

Albumin
Histones
Globulin
Globin
Protamine

25
SImple proteein combined with a non protein components (prosthetic group)
Conjugated protein
26
What are the Conjugated Proteins
Lipoproteins- HDL, LDL, VLDL Chromoproteins- hemoglobin, myoglobin Glycoproteins- mucin, hormones. Metalloproteins- Ferratin, ceruloplasmin. Nucleoproteins -DNA
27
Long and narrow consist of repetitive amino acids sequence. For structural purposes Example: Collagen, fibrin, keratin, actin.
Fibrinous
28
Spherical consist of different amino acid sequence. For functional purposes Example: Enzymes, hemoglobin and hormones.
Globular/globin
29
Classification of proteins based on shape
Fibrinous Globular/globin
30
Classification of proteins based on the solubility soluble in water and concentrated salt solution.
Albumin
31
Classification of proteins based on the solubility insoluble in water and concentrated salt solution but soluble in weak salt solution.
Globulin
32
Classification of proteins based on the solubility insoluble in most reagents Ex. Collagen, elastin, keratin
Albuminoids
33
is used for diagnosing Multiple myeloma and other plasma protein deficiency.
protein electrophoresis
34
Other basis of classification based on molecular size and shape
ULTRACENTRIFUGATION
35
Other basis of classification based on differences in size, shape and charge of protein molecules
CHROMATOGRAPHY
36
Other basis of classification based on differences on molecular volume
GEL FRACTIONATION/MOLECULAR SIEVE