BIOCHEMISTRY 1ST YEAR QUESTIONS AND ANSWERS

BIOCHEMISTRY 1ST YEAR
QUESTIONS AND ANSWERS


All amino acids contain a central carbon, a side chain (R
group), an amino group and a __________ group. - CORRECT
ANSWER-Carboxyl

Amino acids can undergo a proton transfer, thus giving both a
(+) and (-) charge. This molecular state is called the ________.
- CORRECT ANSWER-Zwitterion

Amino acid that are unable to be synthesised from biochemical
pathways within a cell have to be consumed through dietary
intake. These are called _______ amino acids. - CORRECT
ANSWER-Essential

When two amino acids join together, they are joined by an aide
bond. This is also referred to as a _______ bond. - CORRECT
ANSWER-Peptide

Which level of protein structure involves the amino acid
sequence, but not the folding of the protein? - CORRECT
ANSWER-Primary

Unfolding a protein using heat is a process called ________.
This process does not affect the primary sequence of the
protein. - CORRECT ANSWER-Denaturation

If a neutral amino acid is placed in a very basic environment
(pH > 10), it will lose a proton (H+) from the __________
functional group. - CORRECT ANSWER-Carboxyl - COOH

,Disulphides bonds are covalent bonds between two _______
amino acids. - CORRECT ANSWER-Cysteine

The process of breaking the bonds between amino acids within
a polypeptide is called a ______ reaction. - CORRECT
ANSWER-Hydrolysis

All amino acids contain both an acidic carboxyl group and a
basic ______ group. - CORRECT ANSWER-Amino

Amino acids never exist in nature as neutral molecules; rather
they undergo a proton transfer to form a ______. - CORRECT
ANSWER-Zwitterion

Humans are unable to produce _____ of the amino acids
required, and therefore they are referred to as essential amino
acids. - CORRECT ANSWER-10

If an amino acid is placed in a very acidic environment (pH < 2)
which functional group gains a proton (H)? - CORRECT
ANSWER-Carboxyl group

The amino acid at the "ends" of the peptide can be either a N-
terminal amino acid or a ________ amino acid. - CORRECT
ANSWER-C-terminal

Which level of protein structure describes the 3D arrangement
of localised regions? - CORRECT ANSWER-Secondary
structure

Each turn in an alpha helix contains ____ (number) amino acid
residues. - CORRECT ANSWER-3.6

Some enzymes, such as pepsin, break down polypeptides by
______. - CORRECT ANSWER-Hydrolysis

, Various processes, including heating, can achieve disruption of
secondary, tertiary, and even quaternary protein structure. This
type of change in a proteins shape is termed ______ . -
CORRECT ANSWER-Denaturation

There are _____ amino acids that humans must obtain from
diet and can't produce. - CORRECT ANSWER-10

All amino acids contain the acidic _____ group and a basic
amino group - CORRECT ANSWER-Carboxyl

Amino acids never exist in nature as neutral molecules; they
undergo a ______ transfer to from a zwitterion. - CORRECT
ANSWER-Proton

In the Fischer projections when L and D isomers can be
identified by the position of NH3+ group, _____ isomers are
considered common naturally occurring amino acids. -
CORRECT ANSWER-L isomers

If an amino acid is placed in an environment with pH around 6,
they will exist in their ______ form. - CORRECT ANSWER-
Zwitterion

Which structure of protein shows the sequence of amino acids
that form the protein? - CORRECT ANSWER-Primary

______ bonds are covalent bonds that help stabilise the tertiary
structure of protein. - CORRECT ANSWER-Disulfide

The first step in digestion of protein involves some enzymes
such as pepsin in a process called ______. - CORRECT
ANSWER-Hydrolysis

Some enzymes require an additional molecule to be present in
order for the reaction to take place. This additional molecule is
called a ________. - CORRECT ANSWER-Co-factor