Proteins And Their Primary Structure Flashcards

1
Q

List Five Functions of Proteins

A

Enzymes, Hormones, Storage, Transport, Structure, Protective, Contractile, Antibodies

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2
Q

What is the minimum number of residues needed for a protein to fold into its tertiary structure.

A

40

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3
Q

List four physical characteristics that can be used to separate proteins.

A

Solubility
Electrical charge or polarity
Size and Shape
Affinity or Specificity

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4
Q

What are three techniques used for separating proteins based on charge?

A

Ion exchange chromatography
Isoelectric focusing
Electrophoresis

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5
Q

What are three techniques used for separating proteins based on size?

A

Dialysis and ultracentrifugation
Gel electrophoresis
Gel filtration (size exclusion chromatography)

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6
Q

What technique is used to separate proteins based on size and charge?

A

2-D chromatography

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7
Q

What technique is used to separate proteins based on specificity?

A

Affinity chromatography

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8
Q

What three techniques are used to separate proteins based on polarity?

A

Paper chromatography
Reverse-phase chromatography
Hydrophobic chromatography

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9
Q

What is the primary structure of a protein?

A

The particular sequence of amino acids in a protein.

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10
Q

Describe Edman degradation

A

Phenylisothiocyanate labels the the N-terminal end of a peptide chain. This PTH derivative can then be released under acidic conditions, forming a new N-terminal. The process is then repeated.

Cannot be used for peptides longer than 20-30 amino acids.

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11
Q

What are the advantages of Protein ID via Mass Spectrometry?

A

High specificity
High Sensitivity reduces the need for protein purification
Can ID several peptides from the protein at once (High Coverage)
Multiple proteins can be ID’d in a single analysis
Post-translational modifications and locations can be determined.

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