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CLINICAL CHEMISTRY (LEC) > Proteins part 1 > Flashcards

Proteins part 1 Flashcards

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1
Q

Proteins contains how many percent of cell’s dry weight?

A

50-70%

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2
Q

Most abundant macromolecules in the body

A

Proteins

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3
Q

Proteins are expressed in?

A

g/dL

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4
Q

What element differentiates protein from other macromolecules.

A

Nitrogen

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5
Q

Proteins are synthesize in the?

A

Liver

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6
Q

These are produced in the plasma cells

A

Immunoglobulins

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7
Q

positively or negatively charged.

A

Amphoteric

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8
Q

TRUE OR FALSE:
Proteins are water soluble and amphoteric?

A

TRUE

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9
Q

What is the charge of CHON in Alkaline pH?

A

Negative

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10
Q

What is the charge of CHON in Acidic pH?

A

Positive

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11
Q

What type of bond holds the AA together?

A

Peptide bonds / Amide linkages

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12
Q

Give 3 essential AA

A

Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Threonine, Tryptophan and Valine

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13
Q

Refers to the identity and specific order of amino acid residues in the polypeptide chain (amino acid sequence)

A

Primary structure

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14
Q

Determines the overall shape of the protein

A

Primary structure

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15
Q

Refers to the sequence of AA in a peptide or protein

A

Primary structure

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16
Q

Conformation of the segments of polypeptide chain.

A

Secondary structure

17
Q

What are the sheets that composes the secondary structure?

A

Alpha-helix and beta-pleated sheet

18
Q

What type of bond maintains the secondary structure?

A

Hydrogen bond

19
Q

Intramolecular folding of the polypeptide chain into a compact 3-dimensional structure.

A

Tertiary structure

20
Q

This refers to the denaturation of proteins that occurs when temperature change or in the presence of organic solvents or reagents that may change the tertiary structure.

A

Unfolding

21
Q

What type of bond maintains tertiary structure?

A

Covalent Disulfied bond

22
Q

Association of several polypeptide subunits into a larger “oligomeric” aggregate unit.

A

Quaternary structure

23
Q

Incorporation of 2 or more polypeptide chains or subunits into a larger unit

A

Quaternary structure

24
Q

What are the examples of Quaternary structures?

A

Creatine kinase, Lactate dehydrogenase, and Hemoglobin

25
Q

How many subunits does Hemoglobin has?

A

4

26
Q

Proteins can be differentiated based on?

A

A. Differential solubility
B. Molecular size
C. Molecular mass
D. Electrical charge
E. SURFACE ADSORPTION

27
Q

– CHON are affected by pH, ionic strength, temperature and dielectric constant.

A

Differential solubility

28
Q

pH where proteins have no net charge

A

Isoelectric point

29
Q

ions that has 2 different charges but net charge on the molecule is ZERO.

A

Zwitterions

30
Q

Accomplished through ultracentrifugation or dialysis

A

Molecular size

31
Q

Can be accomplished through mass spectrometry

A

Molecular mass

32
Q

Can be accomplished using ion exchange chromatography and electrophoresis.

A

Electrical charge

33
Q

Can be done using chromatography

A

Surface adsorption

34
Q

Between serum and plasma, which one contains Fibrinogen?

A

Plasma

35
Q

Due to the absence of Fibrinogen in serum, the total content decreases into how many percent?

A

4%

CLINICAL CHEMISTRY (LEC) (23 decks)

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