BSC 2010-STEVEN MARKS LATEST
EXAM 1 EXAM QUESTIONS AND
ANSWERS 2026 - 2027
What are some of proteins functions?
structural support, storage, transport, cellular communications,
movement, and defense against foreign substances
polypeptides are
unbranched polymers built from the same set of 20 amino acids
protein
a biological functional molecule that consists of one or more polypeptide
amino acids
organic molecules with carboxyl and amino groups
How do amino acids differ in their properties?
due to differing side chains, called R groups
Amino acids: nonpolar side chains
hydrophobic, mostly hydrocarbons
amino acids: polar side chains
hydrophilic
amino acids: electrically charged side chains
ionic, hydrophilic, either carboxyl or amino groups
Amino acids are linked by
END OF
PAGE
1
, BSC 2010-STEVEN MARKS LATEST
EXAM 1 EXAM QUESTIONS AND
ANSWERS 2026 - 2027
peptide bond
A polypeptide is a polymer of
amino acids
Each polypeptide has a unique linear sequence of
amino acids, with a carboxyl end (C-terminus) and an amino end (N-
terminus)
A functional protein consists of
one or more polypeptides precisely twisted, folded, and coiled into a
unique shape
The sequence of amino acids determines a proteins
three-dimensional structure
primary structure
the sequence of amino acids in a protein, like the order of letters in a
long word (beginning at n-terminus)
secondary structure
result from hydrogen bonds between repeating constituents of the
polypeptide backbone
The only kind of bonds involved in secondary structure of proteins
are
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PAGE
2
, BSC 2010-STEVEN MARKS LATEST
EXAM 1 EXAM QUESTIONS AND
ANSWERS 2026 - 2027
hydrogen bonds
tertiary structure
determined by interactions between r groups, rather than interactions
between backbone constituents
What bonds may reinforce protein structure?
covalent bonds called disulfide bridges
quaternary structure
results when two or more polypeptide chains form one macromolecule
actin
a fibrous protein consisting of chains of actin polypeptides coiled around
eachother
sickle cell disease
Genetic disorder in which red blood cells have abnormal hemoglobin
molecules and take on an abnormal shape.
Which of the following lists some of the levels of biological
organization from less complex to more complex?
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PAGE
3
, BSC 2010-STEVEN MARKS LATEST
EXAM 1 EXAM QUESTIONS AND
ANSWERS 2026 - 2027
atoms, molecules, cells, organs
The innermost electron shell of an atom can hold up to _____
electrons.
2
What relationship is true of an uncharged atom?
The number of protons is equal to the number of electrons.
What determines the types of chemical reactions that an atom
participates in?
the number of electrons in the outermost shell
What is the atomic number of an atom that has 6 protons, 6
neutrons, and 6 electrons?
6
What refers to atoms with the same atomic number but different
atomic masses?
isotopes
Fluorine's atomic number is 9 and its atomic mass is 19. How many
neutrons does fluorine have?
10
An uncharged atom of boron has an atomic number of 5 and an
atomic mass of 11. How many protons does boron have?
END OF
PAGE
4
EXAM 1 EXAM QUESTIONS AND
ANSWERS 2026 - 2027
What are some of proteins functions?
structural support, storage, transport, cellular communications,
movement, and defense against foreign substances
polypeptides are
unbranched polymers built from the same set of 20 amino acids
protein
a biological functional molecule that consists of one or more polypeptide
amino acids
organic molecules with carboxyl and amino groups
How do amino acids differ in their properties?
due to differing side chains, called R groups
Amino acids: nonpolar side chains
hydrophobic, mostly hydrocarbons
amino acids: polar side chains
hydrophilic
amino acids: electrically charged side chains
ionic, hydrophilic, either carboxyl or amino groups
Amino acids are linked by
END OF
PAGE
1
, BSC 2010-STEVEN MARKS LATEST
EXAM 1 EXAM QUESTIONS AND
ANSWERS 2026 - 2027
peptide bond
A polypeptide is a polymer of
amino acids
Each polypeptide has a unique linear sequence of
amino acids, with a carboxyl end (C-terminus) and an amino end (N-
terminus)
A functional protein consists of
one or more polypeptides precisely twisted, folded, and coiled into a
unique shape
The sequence of amino acids determines a proteins
three-dimensional structure
primary structure
the sequence of amino acids in a protein, like the order of letters in a
long word (beginning at n-terminus)
secondary structure
result from hydrogen bonds between repeating constituents of the
polypeptide backbone
The only kind of bonds involved in secondary structure of proteins
are
END OF
PAGE
2
, BSC 2010-STEVEN MARKS LATEST
EXAM 1 EXAM QUESTIONS AND
ANSWERS 2026 - 2027
hydrogen bonds
tertiary structure
determined by interactions between r groups, rather than interactions
between backbone constituents
What bonds may reinforce protein structure?
covalent bonds called disulfide bridges
quaternary structure
results when two or more polypeptide chains form one macromolecule
actin
a fibrous protein consisting of chains of actin polypeptides coiled around
eachother
sickle cell disease
Genetic disorder in which red blood cells have abnormal hemoglobin
molecules and take on an abnormal shape.
Which of the following lists some of the levels of biological
organization from less complex to more complex?
END OF
PAGE
3
, BSC 2010-STEVEN MARKS LATEST
EXAM 1 EXAM QUESTIONS AND
ANSWERS 2026 - 2027
atoms, molecules, cells, organs
The innermost electron shell of an atom can hold up to _____
electrons.
2
What relationship is true of an uncharged atom?
The number of protons is equal to the number of electrons.
What determines the types of chemical reactions that an atom
participates in?
the number of electrons in the outermost shell
What is the atomic number of an atom that has 6 protons, 6
neutrons, and 6 electrons?
6
What refers to atoms with the same atomic number but different
atomic masses?
isotopes
Fluorine's atomic number is 9 and its atomic mass is 19. How many
neutrons does fluorine have?
10
An uncharged atom of boron has an atomic number of 5 and an
atomic mass of 11. How many protons does boron have?
END OF
PAGE
4
