Amino A. structures (L4) Flashcards

1
Q

how significant is example: the valine vs. leucine mutation?

A

Not very significant because both are non-polar

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2
Q

What keeps the alpha helix amino acid held together?

A

Hydrogen bonding

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3
Q

What is an amino acid residue?

A

An amino acid bonded to 2 or more other amino acids (because no longer has same chem structure as before)

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4
Q

In a polypeptide chain, how to know which amino acid it’ll hydrogen bond with

A

add 4, ex: a.a residue #5 is connected to a.a residue #9

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5
Q

How many amino acid resiudes per turn?

A

3.6

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6
Q

Length of 1 turn in an alpha helix?

A

0.34nm

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7
Q

How is the hydrogen bonding formed between?

A

Hydrogen attached to nitrogen and carboxyl group

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8
Q

What holds beta sheets together?

A

Hydrogen bonding

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9
Q

Different configurations of β sheet

A

Antiparallel – backbone run in opposite direction
* Parallel – backbone run in same direction
* Mixed - combination of parallel and antiparallel

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10
Q

What is a single domain protein?

A

A group of beta sheets, or aplha helix sheets (can also be a mix of both)

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11
Q

What is teritary level?

A

When the protein consists of multiple domains
(ex: domain 1 has all alpha,dom 2 has all beta, dom 3 has a mix of both)

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12
Q

What is the quatenary level of proteins?

A

Multiple protein associates together to form a larger, more complex structure

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13
Q

What is domain shuffling?

A

Cutting and recombining different domains to give proteins new functions

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14
Q

What type of molecule is hemoglobin?

A

Heterotetramer

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