1.2 protien Flashcards

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1
Q

protein

A

a biological
macromolecule
composed of amino
acid monomers linked
by covalent bonds

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2
Q

amino acid

A

an organic
molecule composed of
a central carbon atom
bonded to a hydrogen
atom, an amino group,
a carboxyl group, and a
variable R group

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3
Q

why are some amino acids called essential amino acids

A

because they cannot be produced by the human body
and must be consumed as part of the diet. !ese are isoleucine, leucine, lysine, methionine,
phenylalanine, threonine, tryptophan, and valine.

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3
Q

what determines a proteins function

A

The
properties of the side
chains on the amino acids
determine the overall
shape of the protein and,
therefore, its function.

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4
Q

polypeptide

A

a
polymer composed
of many amino acids
linked together by
covalent bonds

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5
Q

the structure of a protein can be divided into four levels of organization. What are they?

A

Primary Structure, secondary, tertiary and Quaternary Structure

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6
Q

what reaction happens in a peptide bond

A

condensation

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7
Q

primary structure fomation

A

sequence of amino acids in a polypeptide chain

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8
Q

secondary structure formation

A

folded structure within a polypeptide due to HB interaction between carbonyl O of one amino acid with the amino H of another. Alpha helix and beta pleated sheet are secondary structures.

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9
Q

Tertiary structure formation ( hard)

A

Most of the protein folding process occurs
naturally as the peptide bonds and the di#erent R groups in a polypeptide chain interact
with each other and with the aqueous environment of the cell. Most of what determines
tertiary structure is the hydrophobic e#ect. For example, polar hydrophilic groups will be
directed toward the aqueous environment, while non-polar hydrophobic groups will tend
to be directed toward the interior of the protein’s three-dimensional shape. !ere are also
other stabilizing forces, such as hydrogen bonding between R groups of di#erent amino
acids and electrostatic attractions between oppositely charged R groups.

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10
Q

quaternary structure formation

A

basically tertiary but with many polypeptide chains (subunits)

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11
Q

Under certain conditions, proteins can completely unfold in a process called?

A

denaturation

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12
Q

when does Denaturation occur

A

when the normal bonding between R groups is
disturbed. Intermolecular bonds break, potentially a#ecting the secondary, tertiary, and
quaternary structures. Conditions that can cause denaturation include extremes of hot
and cold temperatures and exposure to certain chemicals. Once a protein loses its normal
three-dimensional shape, it is no longer able to perform its usual function.

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13
Q
A
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