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

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
Q

SImple proteein combined with a non protein components (prosthetic group)

A

Conjugated protein

26
Q

What are the Conjugated Proteins

A

Lipoproteins- HDL, LDL, VLDL
Chromoproteins- hemoglobin, myoglobin
Glycoproteins- mucin, hormones.
Metalloproteins- Ferratin, ceruloplasmin.
Nucleoproteins -DNA

27
Q

Long and narrow consist of repetitive amino acids sequence.
For structural purposes
Example:
Collagen, fibrin, keratin, actin.

A

Fibrinous

28
Q

Spherical consist of different amino acid sequence.
For functional purposes
Example:
Enzymes, hemoglobin and hormones.

A

Globular/globin

29
Q

Classification of proteins based on shape

A

Fibrinous
Globular/globin

30
Q

Classification of proteins based on the solubility

soluble in water and concentrated salt solution.

A

Albumin

31
Q

Classification of proteins based on the solubility

insoluble in water and concentrated salt solution but soluble in weak salt solution.

A

Globulin

32
Q

Classification of proteins based on the solubility

insoluble in most reagents

Ex. Collagen, elastin, keratin

A

Albuminoids

33
Q

is used for diagnosing Multiple myeloma and other plasma protein deficiency.

A

protein electrophoresis

34
Q

Other basis of classification

based on molecular size and shape

A

ULTRACENTRIFUGATION

35
Q

Other basis of classification

based on differences in size, shape and charge of protein molecules

A

CHROMATOGRAPHY

36
Q

Other basis of classification

based on differences on molecular volume

A

GEL FRACTIONATION/MOLECULAR SIEVE