What methods are used in biotechnology to measure protein concentration? 2. a) W
ID: 208681 • Letter: W
Question
What methods are used in biotechnology to measure protein concentration?
2. a) What is the name of the molecule that constitutes the building block of proteins?
b) How is its name abbreviated?
c) How many different types of those molecules exist?
d)What part of the molecules is similar between all of them?
e) What part is different or unique in each of them?
3. Explain the difference between primary, secondary, tertiary and quaternary protein structures. Give examples.
4. Distinguish between transcription and translation
5. What is the name of the organelle where translation occurs?
Explanation / Answer
Following methods used in biotechnology to measure protein concentration
2. a) Amino Acid constitute the building block of proteins.
b) Abbreviations of amino acids
Full name
3 letter abbrevation
1 letter abbreviation
Alanine
Ala
A
Arginine
Arg
R
Aspargine
Asn
N
Aspartic acid
Asp
D
Glutamic acid
Glu
E
Cysteine
Cys
C
Glutamine
Gln
Q
Glycine
Gly
G
Histidine
His
H
Isoleucine
Ile
I
Leucine
Leu
L
Lysine
Lys
K
Methionine
Met
M
Phenylalanine
Phe
F
Proline
Pro
P
Serine
Ser
S
Threonine
Thr
T
Tryptophan
Trp
W
Tyrosine
Tyr
Y
valine
Val
V
c) There are 20 amino acids exist
d) All 20 of the common amino acids are alpha amino acids.
They have a carboxyl group and an amino group bonded to the same carbon atom that is alpha carbon atom
e) They differ from each other in their side chain or R groups which vary in structure, size and electric charge and which influence the solubility of the amino acids in water
3. The primary structure of a protein refers to the sequence of amino acids in the polypeptide chain. The primary structure is held together by peptide bonds that are made during the process of protein biosynthesis.
Secondary Structure: The Polypeptide chains are organised into regular structures known as alpha-helices (alpha-helixes) and beta-pleated sheets. These are the secondary structures in proteins. These secondary structures are held together by hydrogen bonds.
Tertiary Structure: The overall three-dimensional shape of an entire protein molecule is the tertiary structure. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains may interact and bond in a number of ways.
The quaternary structure refers to how these protein subunits interact with each other and arrange themselves to form a larger aggregate protein complex. The final shape of the protein complex is once again stabilized by various interactions, including hydrogen-bonding, disulfide-bridges and salt bridges.
Eg: Heamoglobin
4. Transcription: it is the synthesis of RNA from DNA template. In the transcription the code in the DNA is converted into a complementary RNA code.
It occurs inside the nucleus in eukaryotes and cytoplasm in prokaryotes
The raw materials are four types of ribonucleoside triphosphates — ATP, GTP. CTP and UTP.
It forms three types of RNAs — rRNA, tRNA and mRNA.
Transcription requires RNA polymerases and some transcription factors.
Polymerase moves over the template.
An adapter molecule is not required,
The product often requires splicing.
The product undergos processing that involves cutting, modification of nitrogen bases, folding and attaching of specific groups at the ends.
Translation: it is the synthesis of a protein from a mRNA template where the code in the mRNA is converted into an amino acid sequence in a protein.
It occurs in the cytoplasm.
The raw materials are 20 types of amino acids.
All the three types of RNAs take part in translation.
Translation requires initiation, elongation and translocase factors.
The ribosome moves over mRNA.
Adapter (= adaptor) molecules bring amino acids over the template.
Splicing is absent.
Processing involves occasional modification of amino acids, combining with other substances (e.g., glycosylation) and packing.
5. Translation occurs in the RIBOSOME
Full name
3 letter abbrevation
1 letter abbreviation
Alanine
Ala
A
Arginine
Arg
R
Aspargine
Asn
N
Aspartic acid
Asp
D
Glutamic acid
Glu
E
Cysteine
Cys
C
Glutamine
Gln
Q
Glycine
Gly
G
Histidine
His
H
Isoleucine
Ile
I
Leucine
Leu
L
Lysine
Lys
K
Methionine
Met
M
Phenylalanine
Phe
F
Proline
Pro
P
Serine
Ser
S
Threonine
Thr
T
Tryptophan
Trp
W
Tyrosine
Tyr
Y
valine
Val
V
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