1.5 Proteins Flashcards

1
Q

Proteins

A

Polymers that have
many subunits (amino acids)
folded into a 3D structure that
determines its function

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2
Q

Most diverse group of molecules in living systems

A

Proteins

There are thousands of different
proteins within your body

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3
Q

Protein Composition

A

Proteins are polymers that are made up of amino acid monomers

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4
Q

Amino Acids made up of…

(building blocks of proteins)

A

A molecule that
consists of a
carboxyl group (COOH), an
amino group (NH2)
and a H atom

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5
Q

How many amino Acids are there

A

There are 20 different types of R Groups and thus 20 different types of amino acids

Differences in the R Groups gives each amino acid different properties

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6
Q

Amino Acid (R Groups) can be

A

R Groups may be positive/negative,
polar/non-polar or may
act as acids/bases

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7
Q

Essential Amino Acids

A

8 Essential Amino Acids

Need to be acquired through diet

Ex. Valine, Leucine, Isoleucine,
Phenylalanine, Tryptophan,
Methionine, Threonine, and
Lysine

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8
Q

Non-Essential Amino Acids

A

12 Non-Essenital amino acids
Amino acids that can be made in
the body

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9
Q

Proteins are built by…

A

Attaching Amino Acids into chains

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10
Q

Amino acids are connected by attaching a –NH2

group to a –COOH group by Dehydration Synthesis

The resulting bond is called a…

A

Peptide Bond

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11
Q

Peptide

A

a term used to describe a chain of amino acids connected with peptide bonds

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12
Q

Polypeptide

A

a peptide with more than 50 amino acids

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13
Q

A protein is one or more polypeptides that are folded into

A

a precise 3D shape

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14
Q

Proteins are only functional after..

A

folding has occurred

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15
Q

Primary Protein Structure

A

Linear sequence of amino acids in polypeptide chain

Changing even ONE amino acid in the chain can alter/destroy the final structure/function of the protein

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16
Q

Secondary Protein Structure

A

The coiling/folding of amino acid chain

Occurs because of hydrogen bonding between different amino acids

Beta-pleated sheet (zig-
zag like pattern) and
Alpha-helix (spiral
pattern) are two
common secondary
structures

17
Q

Tertiary Protein Structure

A

Folding of the protein into a
3D shape caused by R-group
interactions

Intermolecular reactions (e.g.,
ionic bonds, hydrogen bonds,
etc.) of the R-groups determine the 3D shape
Tertiary structure is critical to
the function of proteins,
especially enzymes

18
Q

Quaternary Structure

A

Linking several separate
polypeptide chains
together

E.g., hemoglobin is made
of 4 polypeptides

19
Q

Protein Prosthetic Groups

A

Proteins can also bond with non-protein structures, called prosthetic groups, in order to
function

Many enzymes require prosthetic groups that
contain metal ions to function