Lecture 4-7 Flashcards

1
Q

Essential Amino Acids

A

Histidine, Isoleucine, Leucine, Lysine, Phenylalanine, Threonine, Tryptophan, Valine

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2
Q

Essential Amino Acids where consumption > production

A

Arginine, Methionine

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3
Q

Nonessential Amino Acids

A

Alanine, Asparagine, Aspartic acid, Cysteine, Glutamine, Glutamic acid, Glycine, Proline, Serine

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4
Q

Secondary Synthesis

A

Tyrosine

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5
Q

What is the only amino acid that can participate in Redox reactions

A

Cysteine

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6
Q

Proteinogenic Amino Acid

A

Used to make proteins from the genetic code

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7
Q

Nonproteinogenic Amino Acids

A

Not decoded from the genome

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8
Q

What is considered the 21st Amino Acid

A

Selenocysteine

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9
Q

What is Selenocysteine synthesized from

A

Serine

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10
Q

What is considered the 22nd Amino Acid

A

Pyrrolysine

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11
Q

What is pyrrolysine synthesized from

A

Combining 2 lysines

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12
Q

Where is pyrrolysine found

A

Only in prokaryotes all of which are methanogens

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13
Q

A deficiency in what amino acid causes statin intolerance and how

A

Selenium- statins inhibit tRNA that form selenocysteine

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14
Q

How are most antibiotics made

A

Non-ribosomal protein synthesis

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15
Q

Protein Primary structure

A

A chain of amino acids

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16
Q

Protein Secondary structure

A

Local folding of the polypeptide chain, connected by hydrogen bonds

17
Q

Protein Tertiary structure

A

Folding of the secondary structure, connected by disulfide linkages

18
Q

Protein Quaternary structure

A

Interaction of multiple peptides

19
Q

Non-covalent interactions that govern protein folding stability

A

Van der Waals- short range repulsion, Hydrogen Bonds, Electrostatic forces

20
Q

With what elements are Hydrogen bonds possible

A

Nitrogen, Oxygen, Flourine

21
Q

What direction turn is more energetically favored in an alpha-helieces

A

Right-handed or clockwise

22
Q

How are beta sheets stabilized

A

Hydrogen bonding between polypeptide strands

23
Q

What direction can beta sheets run

A

Parallel and antiparallel

24
Q

What protein structure serves predominantly in a structural manner

A

Superhelix

25
Q

What is a hallmark structure of a superhelix

A

300 amino acid that contains heptad repeats

26
Q

What is an intermediate conformational state between the native and the fully unfolded states of a globular protein

A

Molten Globule State

27
Q

How much larger is the molten globule state vs native state

A

10-30%