Clin-Chem Lab AA Part 2

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27 Terms

1

Structural Organization of Proteins

Primary Structure

Secondary Structure

Tertiary Structure

Quaternary Structure

<p>Primary Structure</p><p>Secondary Structure</p><p>Tertiary Structure</p><p>Quaternary Structure</p>
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2

Structural Organization of Protein wherein it has:

Linear sequence of Amino Acids joined by peptide bonds.

• The order is determined by DNA sequence.

Primary Structure

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3

In this type of protein structure the peptide bond is between the carboxyl group of amino acid “A” and amino group of amino acid “B”.

Primary Structure

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4

Protein example of Primary Structure

Insulin

<p>Insulin</p>
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5

Structural Organization of Protein wherein it is:

Formed by hydrogen bonds between:

• Carbonyl (C=O) and Amino (N-H) groups of peptide backbones.

• Creates specific folding patterns.

Secondary Structure

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6

A secondary structure of protein that is a right-handed spiral.

Alpha helix

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7

A secondary structure of protein wherein polypeptide chains are arranged side by side (parallel/ antiparallel)

Beta Pleated Sheet

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8

Protein example of Secondary Structure

Keratin (Alpha helix)

Silk Fibroin (Beta Pleated Sheet)

<p>Keratin (Alpha helix)</p><p>Silk Fibroin (Beta Pleated Sheet)</p>
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9

Structural Organization of Protein wherein it has:

• Overall 3D shape of a single polypeptide chain.

• Formed by interactions between R groups side chains of amino acids.

Tertiary Structure

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10

What are the types of Bonds under Tertiary Structure

• Hydrogen Bonds

• Ionic Bonds (Salt Bridges)

• Disulfide Bonds

• Hydrophobic Interactions

• Van der Waals Forces

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11

• Hydrogen Bonds →

• Ionic Bonds (Salt Bridges) →

• Disulfide Bonds →

• Hydrophobic Interactions →

• Van der Waals Forces →

• Hydrogen Bonds → polar side chains

• Ionic Bonds (Salt Bridges) → between + & - R group

• Disulfide Bonds → covalent bonds

• Hydrophobic Interactions → nonpolar side chains

• Van der Waals Forces → weak interactions of atoms

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12

Protein example of Tertiary Structure

Lysozyme

Myoglobin

<p>Lysozyme</p><p>Myoglobin</p>
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13

Structural Organization of Protein wherein it has:

Multiple polypeptide chains (subunits) that interact to form a functional protein complex.

Quaternary Structure

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14

Types of Quaternary Structure

• Homodimer/ Heterodimer → 2 subunits (identical/ different)

• Tetramer → 4 subunits

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15

Protein example of Quaternary Structure

Hemoglobin

Immunoglobin

<p>Hemoglobin</p><p>Immunoglobin</p>
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16

Oxygen transport protein, carries oxygen from lungs and delivers to tissue sites. (Has Alpha and Beta Chains)

Hemoglobin

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17

Antibody protein.

Immunoglobulin

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18

Tests/ Procedures on protein. (Protein Methodologies)

Tests/ Procedure:

• Total protein

• Albumin

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19

Sample of choice on protein tests?

Serum (Absence of fibrinogen)

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20

Why is Serum preffered than Plasma?

Plasma contains coagulation factors (fibrinogen) that can interfere with the results.

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21

Is fasting required, on protein tests?

No, because proteins don’t get metabolyzed that fast compared to lipids.

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22

Interferences in specimen considerations?

Interferences:

• Lipemia (excess lipids in blood)

• Hemolysis (presence of hemoglobin)

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23

Can slight hemolysis still be run as a sample?

Yes, but place a note on the request form.

<p>Yes, but place a note on the request form.</p>
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24

Can Moderate and Gross hemolysis still be run as a sample?

No (big changes).

<p>No (big changes).</p>
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25

The Tests under Protein Methodologies

• Total protein

• Albumin

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26

Methods under Total protein. (Protein Methodologies)

KJELDAHL

BIURET

DYE BINDING

REFRACTOMETRY

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27

Methods under Albumin. (Protein Methodologies)

SALT PRECIPITATION

DYE BINDING

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