Chapter 7.1 Proteins Flashcards

1
Q

Similarities and differences in amino structures?

A

All contain amino acids but the sequence itself is unique to every structure.

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2
Q

What happens during denaturation?

A

Disrupts H and ionic bonds. Uses heat, pH levels, and salinity.

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3
Q

What is a hydrophobic interaction?

A

Clusters away from water.

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4
Q

What is a hydrophilic interaction?

A

Forms hydrogen bonds.

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5
Q

What is an acidic and basic interaction?

A

Forms ionic bonds.

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6
Q

What is a cysteine interaction?

A

Forms disulfide bonds.

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7
Q

What do these interactions have to do with the tertiary level?

A

They create the final shape of the structure.

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8
Q

What are some examples of protein types and their functions?

A

Storage: bean storage proteins
Movement: muscle fibers
Transport: through channels and pumps
Identification: cell surface proteins(labels)
Defense: Antibodies that recognize the labels.
Chemical reactions: enzymes
Structure: keratin and collagen
Communication: Hormones and receptors

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9
Q

Why and how would the structure and function of a protein change if a hydrophobic amino acid was substituted for a hydrophilic one?

A

it would change how the structure is folded to meet all the criteria for each amino acid, so the hydrophilic are on the outside, hydrophobic go inwards, etc.

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10
Q

What is the first level of the protein structure?

A

Primary - Order of amino acids, unique sequence

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11
Q

What is the second level?

A

Secondary- Folding of beta pleated sheets and alpha helixs.

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12
Q

Third level?

A

Tertiary - Interactions between side chains and amino acids. The 3D shape of a single polypeptide.

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13
Q

What is the fourth level?

A

Quaternary - More than one polypeptide bonded together.

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