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Biology
Topic 2 genes and health
2. Proteins
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Cards (56)
What are the functions of proteins?
Catalyze reactions (
enzymes
)
Transport molecules (
carrier proteins
)
Defend against disease (
antibodies
)
Support cells and tissues (
structural proteins
)
Transmit information (
hormones
)
Carry oxygen (
transport proteins
)
Enable muscle contraction (
contractile proteins
)
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Why can proteins perform a wide range of biological functions?
Each protein has a specific
molecular
shape
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What is the basic structure of an amino acid?
Carboxyl group
(-COOH)
Amino group
(-NH2)
Central carbon atom
(C)
Variable group
(R)
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How many different naturally occurring amino acids are there?
20
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What is the primary structure of proteins?
The order of
amino acids
in a chain
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What are proteins made up of?
C
,
H
,
O
,
N
, and some
S
and
P
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What happens during a condensation reaction between amino acids?
A water molecule is removed, forming a
peptide bond
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What is the bond called that joins two amino acids?
Peptide bond
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What is hydrolysis in relation to proteins?
Addition of water that breaks
peptide bonds
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What are the four structural levels of proteins?
Primary structure: sequence of
amino acids
Secondary structure: initial folding (
alpha helix
,
beta pleated sheet
)
Tertiary structure:
3D shape
from R-group interactions
Quaternary structure: multiple
polypeptide chains
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What type of bonds are present in the secondary structure of proteins?
Hydrogen bonds
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What maintains the tertiary structure of proteins?
Interactions between
R-groups
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What is the role of disulfide bridges in proteins?
Provide
further
support
to the
protein
structure
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What is quaternary structure in proteins?
Multiple
polypeptide
chains working together
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What types of bonds hold the four structural levels of proteins together?
Peptide bonds
(primary)
Hydrogen bonds
(secondary and
tertiary
)
Ionic bonds (tertiary)
Disulfide bonds
(tertiary)
Hydrophobic and hydrophilic interactions (tertiary)
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What happens to ionic bonds in proteins when pH changes?
They can be split by changing pH
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What defines the R group in amino acids?
It
varies
among different
amino
acids
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How do amino acids act as buffers?
They can accept or release
H+
ions
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What is the reaction that joins two amino acids together?
Condensation reaction
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What determines the final 3D structure of a protein?
The interactions between
R-groups
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What are the four structural levels in proteins?
Primary
,
secondary
,
tertiary
,
quaternary
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What type of bond holds the primary structure of proteins together?
Peptide bonds
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Which bonds are involved in the secondary and tertiary structures of proteins?
Hydrogen bonds
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What types of bonds are found in the tertiary structure of proteins?
Ionic,
disulphide
, hydrogen
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What does the quaternary structure of a protein depend on?
The 3D structure of individual
polypeptides
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What are the two groups found in all amino acid molecules?
Amine group
and
carboxyl group
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What reaction joins amino acids together in proteins?
Condensation reaction
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What determines the final 3D structure of a protein?
The order of
amino acids
in the
primary sequence
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How does a secondary structure become a tertiary structure?
Through interactions between
R-groups
of
amino acids
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What are the two main groups of proteins?
Globular proteins
and
fibrous proteins
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Why are globular proteins soluble in water?
Due to hydrophilic R groups that point outwards
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What is the role of enzymes in metabolic reactions?
They catalyze
intracellular
reactions
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What is the structure of hemoglobin?
It has 4
polypeptide
chains
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How does the structure of hemoglobin contribute to its function?
Hydrophilic side r groups outwards for solubility
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What type of protein is collagen?
Fibrous protein
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What is the overall structure of fibrous proteins?
They form long
chains
or fibers
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Why are fibrous proteins insoluble in water?
Due to their
fibrous
nature
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What is the role of collagen in living organisms?
Provides strength and support to tissues
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How do the structures of collagen and hemoglobin differ?
Collagen is
fibrous
, hemoglobin is
globular
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What stabilizes the structure of collagen?
Covalent cross-links
between collagen molecules
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