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BIOL 1107 EXAM #1 STUDY GUIDE QUESTIONS WITH COMPLETE SOLUTIONS

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BIOL 1107 EXAM #1 STUDY GUIDE QUESTIONS WITH COMPLETE SOLUTIONS

Institution
BIOLOGY 1107
Course
BIOLOGY 1107

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BIOL 1107 EXAM #1 STUDY GUIDE
QUESTIONS WITH COMPLETE
SOLUTIONS
Each polypeptide has a free carboxyl group at one end, called the ____ or ____
terminal. - ANSWER-C or carboxyl

a polymer of amino acids - ANSWER-polypeptide

polypeptides that have combined together, often have bound not-peptide prosthetic
groups, have a distinct shape, and have a unique function. - ANSWER-protein

After protein synthesis (translation), most proteins are modified. These are known as
____. They may undergo cleavage, phosphorylation, or may require the addition of
other chemical groups. Only after these modifications is the protein completely
functional. - ANSWER-post-translational modifications

An enzyme can bind to a specific substrate at a site known as the ____. - ANSWER-
active site

the unique sequence of amino acids in a poly peptide chain is its ____. - ANSWER-
primary structure

The most common secondary structures of a protein (held together by hydrogen
bonds) - ANSWER-α-helix and β-pleated shhet

The local folding of the polypeptide in some regions gives rise to the ____ of the
protein. - ANSWER-secondary structure

How does the hydrogen bonding happen in an alpha helix? - ANSWER-between the
oxygen atom in the carbonyl group in on amino acid and another amino acid that is
four amino acids farther along the chain

The unique three-dimensional structure of a polypeptide is its ____. - ANSWER-
tertiary structure

What is the tertiary structure of a protein primarily caused by? - ANSWER-the
interactions among R groups (can counteract hydrogen bonds of secondary
structures- hydrophobic R groups lay in the interior of the protein whereas the
hydrophilic R groups lay on the outside)

What is the only covalent bond formed during protein folding? - ANSWER-disulfide
bonding between cysteine side chains

All proteins are made up of different arrangements of the same ____ types of ____. -
ANSWER-20, amino acids

, ____ are the monomers that make up proteins - ANSWER-amino acids

Each amino acid has the same fundamental structure which consists of - ANSWER-
a central carbon atom (alpha carbon) bonded to an amino group (NH2), a carboxyl
group (COOH), to a hydrogen atom, and an R group.

The name "amino acid" is derived from - ANSWER-the fact that they contain both
amino group and carboxyl-acid-group in their basic structure.

For each amino acid, the ____ is different. - ANSWER-R group (or side chain)

The chemical nature of the ____ determines the nature of the amino acid (whether it
is acidic, basic, polar, or non polar). - ANSWER-side chain

Positively charged side chains of amino acids make them ____ amino acids. -
ANSWER-basic

Proline is an exception to the standard structure of an amino acid since - ANSWER-
its amino group is not separate from the side chain

____ amino acids refer to those necessary for construction of proteins in the body;
varies from organism to organism. - ANSWER-Essential

Each amino acid is attached to another acid by a ____ known as a ____. -
ANSWER-covalent bond, peptide bond

In a peptide bond, the ____ group of one amino acid and the ____ group of the
incoming amino acid combine, releasing a molecule of ____. This is formed by a
____. - ANSWER-carboxyl, amino, water, dehydration reaction

The products formed by peptide bonds are called ____ and a chain of these are
____. - ANSWER-peptides, polypeptides

Each poly peptide has a free amino group at one end, called the ____ or ____
terminal. - ANSWER-N or amino

The tertiary structure of proteins is determined by a variety of chemical interactions
including: - ANSWER-hydrophobic interactions, ionic bonding, hydrogen bonding,
and disulfide linkages

The interaction of several polypeptides, or subunits, forms the ____ of a protein. -
ANSWER-quaternary structure

When a protein loses its shape without losing its primary sequence; often reversible;
sometimes irreversible leading to loss of function; can be caused by changes in
temperature or pH - ANSWER-denaturation

protein helpers that associate with the target protein during the folding process -
ANSWER-chaperones

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Institution
BIOLOGY 1107
Course
BIOLOGY 1107

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