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Cards (86)
What are the three main macromolecules in biochemistry?
Proteins
,
lipids
, nucleic acids
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Why are enzymes important in biochemistry?
They act as
biological
catalysts and
drug targets
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What does biochemistry study?
Atoms
and
molecules
in living organisms
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How does biochemistry bridge biology and chemistry?
By explaining
molecular mechanisms
of
life processes
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What are biological macromolecules?
Structures that provide
cell structure
and functions
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How does biochemistry help in medicine?
Advancements in
drug development
and
diagnostics
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What elements are essential for life?
Carbon
,
Hydrogen
, Oxygen,
Nitrogen
,
Phosphorus
,
Sulphur
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How many chemical elements occur naturally in plants and animals?
About 31
elements
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What percentage of the dry weight of living things is made up of C, H, O, N, P, and S?
About
92%
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What are trace elements in biological material?
Elements in small quantities
essential
for life
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What is the zwitterion form of amino acids?
Amino acids with both
positive
and
negative
charges
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What happens to the carboxylic acid group in zwitterions?
It donates a
proton
to the amino group
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How are amino acids esterified?
By
heating
with alcohol and
sulfuric acid
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What is the result of acylation of the amino group?
Conversion to an amide with
acylating agents
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What occurs when amino acids react with strong acids?
They behave as
bases
and form
positive ions
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What occurs when amino acids react with strong alkalis?
They behave as acids and form negative
ions
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What color indicates the presence of amino acids in the Ninhydrin test?
Purple
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What is a protein?
A
biological
polymer
made of
amino acids
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What are the functions of proteins?
Structure
,
catalysis
, movement, transport,
hormones
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How many different amino acids are used to build proteins?
Twenty
different amino acids
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What is a peptide bond?
A bond linking two
amino acids
together
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What is the N-terminus of a peptide chain?
The end with the
amine group
(NH2)
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How is the amino acid sequence of a peptide displayed?
Amino terminal
end on the left,
carboxyl
on the right
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What defines primary protein structure?
Covalent peptide bonds
forming a
polypeptide chain
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What can mutations in the amino acid sequence affect?
Protein folding
and function
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What is secondary protein structure characterized by?
Hydrogen bonding between
peptide bonds
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How is an α-helix formed?
By
hydrogen bonding
between
peptide bonds
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What characterizes a β-pleated sheet?
Hydrogen bonds
between
amino acids
on different sheets
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What is tertiary protein structure?
Folding of the
polypeptide
chain into
3D
shape
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What can disrupt tertiary protein structure?
Disruption of bonds between
R groups
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What is protein denaturation?
Loss of protein
shape
and
function
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What types of bonds are involved in tertiary protein structure?
Hydrogen
,
electrostatic
, covalent,
hydrophobic
bonds
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What is quaternary protein structure?
Linking of multiple
polypeptide
chains
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What is the role of fully functional proteins?
Perform
specific roles
within
the
body
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What is an enzyme?
A
protein
that
catalyzes
biological reactions
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How do enzymes affect activation energy?
They
lower
the
activation
energy
of
reactions
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What factors affect enzyme activity?
pH, enzyme concentration, substrate
concentration
, temperature
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What is enzyme-substrate specificity?
Enzymes
bind specifically to their
substrates
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What is the active site of an enzyme?
A specific region that binds to the
substrate
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What happens to the substrate in the presence of an enzyme?
It is modified to produce a
product
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