Chapter 3: Amino acid protein structure, purification, & analysis Flashcards

1
Q

Proteins are what?

A

Peptides with an amino acid sequence directed by the genetic code

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2
Q

How many possibilities are there for the primary structure of amino acids?

A

20^n possibilities (n= to the # of amino acids)

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3
Q

The secondary & tertiary structure of proteins are what?

A

3D functional shape

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4
Q

Quaternary structure is what?

A

Multiple folded polypeptides in a protein

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5
Q

Proteomics

A

Study of cellular protein complement over time & varying conditions

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6
Q

Conjugated proteins

A

Are proteins that contain more than just amino acid group where coenzymes and prosthetic groups are bound to proteins and required for protein function (ex. lipoproteins where lipids is its prosthetic group)

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7
Q

Most studies & assays require protein purity of how much percent?

A

95-98%

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8
Q

What is the common technique used for protein separation

A

Chromatography

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9
Q

What are all the fractioning techniques?

A
  1. Salting out
  2. Ion exchange chromatgraphy
  3. Gel electrophoresis
  4. Isoelectric focusing
  5. Hydrophobic ineteraction
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10
Q

Proteins are least soluble when?

A

At the pI

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11
Q

Proteins are net positively charged when?

A

At pH below pI

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12
Q

Proteins are net negatively charged when?

A

Above the pI

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