Task 2 Biochemistry

Topics: Protein, Amino acid, Secondary structure Pages: 13 (831 words) Published: March 20, 2015
Biochemistry, GRT1
Task 2

Essential Amino Acid Valine

A1: 2 Characteristics of Valine
• Valine is a nonpolar amino acid, with many carbons
surrounded by hydrogen. Valine is unable to interact
with water molecules, making it HYDROPHOBIC (MSDS,
2005).
• Flammability- Valine is combustible at high
temperatures. These products are carbon oxides and
nitrogen oxides. In case of a small fire, dry chemical
powder should be utilized. In case of a large fire, utilize
water spray, fog or foam. No water jets (MSDS, 2005).
• Valine is slightly toxic to humans in cases of ingestion and inhalation. Valine also crosses the placental barrier
(MSDS, 2005).

B. Levels of protein Structures
Primary

• DNA makes RNA, RNA Protein
• Proteins are polypeptides- which are chains of
Amino Acids
• RNA instructs the assignment of the amino acids
• The primary structure of a protein is the order
and organization of the amino acids (Wolf, 2009).

B. Levels of protein Structures
Secondary
• Secondary structure is due to
hydrogen bonding between the
amino acids
• The alpha helix a secondary
bond, which forms a coil
through a hydrogen bonds
between every 4th amino acid
(Wolf, 2009).
• A beta pleated sheet, is also
another secondary bond,
formed with hydrogen bonds
bringing together 2 adjacent
segments

B. Levels of protein Structures
Tertiary
• A tertiary structure is the 3D
structure of the protein
• R groups interacting
• Different secondary structures
(helix and pleats) fold up to
make the final shape of a
protein
• The 3D shape determines a
proteins function- such as
prions, myoglobin (Wolf, 2009)
• There are 4 types of bonds
which form tertiary interactions:
1. Hydrophobic/nonpolar- the
weakest
2. Hydrogen/polar
3. Ionic bond
4. Disulfide bond- 2 cysteine
Amino acids

B. Levels of protein Structures
Quaternary
• Quaternary structure is when there’s interaction
between more than one polypeptide, such as
hemoglobin.

C. A Peptide Bond through
Dehydration
• 2 amino acids come
together through the
process of dehydration
• During the process, a
H+ atom is lost from
the amine group & –
OH is lost from the
carboxyl group= loss
of a water molecule
• A covalent bond is
forms between the
two amines (HudsonMiller, ND).

D. Breaking a Dipeptide Bond
Through Hydrolysis
• The dipeptide bond is
broken by adding a
water molecule.
• The OH- combines
with the carboxyl end
of one amino acid,
while the hydrogen
attaches to the
nitrogen/amine side
of the other amino
acid, splitting the
dipeptide bond into
two separates
(Hudson-Miller, ND).

E. Stabilization of Protein @
the Tertiary Level
• The tertiary level deals with R groups interactions,
of which there are 3 types; polar, nonpolar &
charged
• There are 4 types of R group interactions:
1. Hydrophobic/nonpolar, where the R group cluster
on the inside of the protein because they don’t
like water.
2. Van der Waals interactions are weak interactions
that take place between tightly wound nonpolar
R groups, on the inside of the protein, due to
charge fluctuations within the molecule.
3. Ionic bonds occur between positive and negative
R groups

Bovine Spongiform Encephalopathy
at Molecular Level F1-F3
• At the molecular level, Bovine Spongiform
Encephalopathy (BSE) is an infectious protein, also known
as a prion, known as PrPsc.
• PrPsc transfers bad information to the healthy protein,
which is known as PrPc.
• PrPc then becomes hydrophobic and misfolds.
• PrPsc has taken on the role of a chaperone. The role of a chaperone in the case of the prion is one that influences
the PrPc to take on the role of PrPsc (Thompson, ND)
• The proteins cannot be corrected after conversion, and
they aggregate, sticking to one another after conversion
in great numbers, thus becoming spongy tissue and
causing cell death (Thompson, ND) .

F4. Recommendations for
Countries without BSE Regulations
•...
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