Chapter 4 Flashcards

1
Q

What are the 4 levels of protein structures?

A

Primary
Secondary
Tertiary
Quaternary

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2
Q

How are Amino Acids joined?

A

Covalently through peptide bonds

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3
Q

What do Peptide bonds consist of?

A

Carboxyl Group and Amino Groups

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4
Q

What does the denature of the protein do and at which level does this occur at?

A

disrupt structure and function

tertiary

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5
Q

What are the roles of Amino Acids?

A
Enzymes
Storage and Transport
Cell shape
Decode cell info
Horomones
Receptors
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6
Q

Protein diversity

A

Dependent on complexity of organism

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7
Q

How can Freedom of rotation be decreased?

A

With Double or triple Bonds

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8
Q

The lowest Delta G means what in proteins?

A

Most stable form

Max number of weak interactions

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9
Q

What are the steps of protein folding?

A

1) Secondary Structures form
2) Hydrophobic core condenses
3) Tertiary Structure

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10
Q

What do peptide chains have the ability to do?

A

Add on amino acids duo to it being uncharged

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11
Q

φ

A

phi, between N amino group and the α-carbon

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12
Q

Ψ

A

psi, between α-carbon and carbonyl carbon (COO-)

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13
Q

Ramachandran Plot

A

Tells you allowable combinations of φ and Ψ and how the fold

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14
Q

Primary Structure

A

linear amino acid sequence,

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15
Q

Secondary Structure

A

localized interactions within the polypeptide

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16
Q

What is the Main Chain?

A

Hydrogen bonds between the amino and carboxyl

17
Q

What is folding restricted by?

A

Flexibility of bonds

18
Q

Tertiary Structure

A

the final structure of a single polypeptide

19
Q

Quaternary Structure

A

the structure of multiple small polypeptide sub units coming together