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Problem Set 2 Proteins

This document provides information about protein structure and function. It defines primary, secondary, and tertiary protein structure. It discusses how hemoglobin's quaternary structure arises from interactions between its tertiary structures. The document also explains how coiling of polypeptide chains and higher-level protein structures provide protection from denaturation. It addresses biological functions of specific amino acids and how reducing agents and alcohol are used to treat bacteria.

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Justine Escobal
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156 views4 pages

Problem Set 2 Proteins

This document provides information about protein structure and function. It defines primary, secondary, and tertiary protein structure. It discusses how hemoglobin's quaternary structure arises from interactions between its tertiary structures. The document also explains how coiling of polypeptide chains and higher-level protein structures provide protection from denaturation. It addresses biological functions of specific amino acids and how reducing agents and alcohol are used to treat bacteria.

Uploaded by

Justine Escobal
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as DOC, PDF, TXT or read online on Scribd
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Meg Erica Gilua BSMT 2A

PROBLEM SET 2
PROTEINS

1. Identify the specific parts of primary, secondary, and tertiary structures in the
numbered boxes:

1) a-Carboxyl group
2) a-Amino group
3) B-pleated sheet: anti-parallel intermolecular
4) Random coil
5) Hydrophobic interaction
6) Disulfide bridge
7) a–helix formed by hydrogen bonds
8) Ionic bond
9) Hydrogen bond

2. Which structural features in hemoglobin are the primary, secondary, tertiary and
quaternary structure?
- The quaternary structure of a hemoglobin molecule includes four tertiary structure
protein chains, which are all alpha helices. Individually, each alpha helix is a
secondary polypeptide structure made of amino acid chains. The amino acids are
in turn the primary structure of hemoglobin.

3. Explain the biological function achieved by the coiling of polypeptide chains as well
as the coiling of higher levels of structures of proteins such as keratin and
collagen. Is there any advantage to having successive levels of structure coiled in
opposite directions?
- The biological function achieved by the coiling of polypeptide chains is to provide
protection from denaturation by forming an insoluble structure due to the non-polar
R groups pointing outside and covering the coil making.

4. Which amino acid side chain is most frequently involved in denaturation by


reduction?
- a-carboxyl group & a-amino group (???)

5. What does the reducing agent do in straightening curly hair?


- The reducing agents in hair-straightening products break down the disulphide
bonds in hair. This softens the hair and allows it to be pulled straight.

6. Silver nitrate is sometimes put into the eyes of newborn infants as a preventive
measure against gonorrhea. Silver is a heavy metal. Explain how this treatment
may work against bacteria.
- Before health professionals had antibiotics to treat infections, they put silver nitrate
in babies’ eyes to prevent gonorrhea from causing corneal infections and turning
babies blind. Silver nitrate is a surface-active chemical that facilitates agglutination
and inactivation of gonococci.
- Silver nitrate has shown different effects against bacteria as at high concentrations,
killing bacteria by different mechanisms, which are: binding to the thiol groups of
protein and denaturing them, programmed cell death (apoptosis) and causing the
DNA to be in the condensed form (not in the relaxed form), which inhibits cell
replication. At lower concentrations, it induces them to synthesize silver
nanoparticles.

7. Why do nurses and physicians use 70% alcohol to wipe the skin before giving
injections?
Nurses and physicians use 70% alcohol to disinfect the skin prior to injections to
prevent infections by bacteria on the skin. 70% alcohol solutions coagulate the
proteins but at a slower rate compared to the 95% concentration. Hence, it
penetrates the cell wall more completely which permeates the entire cell,
coagulates all proteins, and therefore the microorganism dies.

Pure alcohol coagulates protein in contact. Suppose the pure alcohol is poured
over a single celled organism. The alcohol will go through the cell wall of the
organism in all direction, coagulating the protein just inside the cell wall. The ring of
the coagulated protein would then stop the alcohol from penetrating farther from
the cell, and no more coagulation would take place. At this time the cell would
become inactive but not dead.
8. Why is it important to specify the 3-D structure of amino acid?
- Because (1) the three-dimensional structure of a protein is determined by its amino
acid sequence, (2) the function of a protein depends upon its three-dimensional
structure, (3) the three-dimensional structure of a protein is unique, (4) to
recognize several common patterns.
- Polypeptides with very different amino acid sequences sometimes assume similar
structures, and similar amino acid sequences sometimes yield very different
structures.
9. Three test tubes contain 2% albumin solution. One drop of 1N acid is added to the
st nd
1 test tube and 2 drops of 5N acid to the 2 test tube. The third test tube serves
as control. Theoretically, which test tube do you think has the best coagulation
when heated? Explain your answer.

10. A solution of albumin forms precipitate with silver nitrate. Another test tube
containing same sample of albumin but few drops of 0.1N NaOH were added
before adding the silver nitrate. Which has more precipitate, the test tube with or
with out NaOH? Explain
11. What is the test that differentiates peptone from albumin? Explain.
12. What will you do to detect the presence of P in powdered casein? Briefly explain
each process.

Marnan T. Libres, M.Chem


Instructor

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