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BIO192Sciences2 Unitsintermediate

General Practical Biology II

This course, General Biology Practical II, covers the chemistry of amino acids and proteins, focusing on the building blocks of proteins and their polymers. It explores the structural features of these molecules and their impact on biological activity. The course aims to develop a greater comprehension of how the structures of biomolecules affect their overall cellular functions, covering topics such as amino acids, peptides, and proteins.

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39h
Study Time
13
Weeks
3h
Per Week
basic
Math Level
Course Keywords
Amino AcidsPeptidesProteinsEnzymesBiochemistry

Course Overview

Everything you need to know about this course

Course Difficulty

Intermediate Level
Builds on foundational knowledge
65%
intermediate
➕
Math Level
Basic Math
🔬
Learning Type
Hands-on Practice

Course Topics

Key areas covered in this course

1

Amino Acids

2

Peptides

3

Proteins

4

Enzymes

5

Protein Structure

6

Protein Stability

7

Protein Purification

8

Amino Acid Chemistry

Total Topics8 topics

Ready to Start

No specific requirements needed

This course is designed to be accessible to all students. You can start immediately without any prior knowledge or specific preparation.

Assessment Methods

How your progress will be evaluated (3 methods)

assignments

Comprehensive evaluation of course material understanding

Written Assessment

tutor-marked assignments

Comprehensive evaluation of course material understanding

Written Assessment

final examination

Comprehensive evaluation of course material understanding

Computer Based Test

Career Opportunities

Explore the career paths this course opens up for you

Biochemist

Apply your skills in this growing field

Research Scientist

Apply your skills in this growing field

Laboratory Technician

Apply your skills in this growing field

Pharmaceutical Scientist

Apply your skills in this growing field

Food Scientist

Apply your skills in this growing field

Industry Applications

Real-world sectors where you can apply your knowledge

PharmaceuticalsBiotechnologyFood IndustryResearch LaboratoriesHealthcare

Study Schedule Beta

A structured 13-week journey through the course content

Week
1

Module 1: Amino Acids

2h

Unit 1: Amino Acids as Building Blocks of Proteins

2 study hours
  • •Define amino acids and their role as building blocks of proteins.
  • •Explain the occurrence of amino acids in nature.
  • •Understand the concepts of chirality and stereoisomerism.
  • •Practice writing the structures of common amino acids.
Week
2

Module 1: Amino Acids

2h

Unit 2: Classification of Amino Acids

2 study hours
  • •Classify amino acids based on their structures and functional groups.
  • •Identify polar and nonpolar amino acids.
  • •Understand the nutritional requirements of amino acids.
  • •Draw and recognize the structures of all common amino acids.
Week
3

Module 1: Amino Acids

2h

Unit 3: Properties of Amino Acids

2 study hours
  • •Discuss the physical properties of amino acids, including their response to heat.
  • •Explain the optical activity of amino acids and its significance.
  • •Understand the absorption of light by amino acids.
  • •Describe the acid-base properties of amino acids.
Week
4

Module 1: Amino Acids

2h

Unit 4: Chemical Reactions of Amino Acids

2 study hours
  • •Discuss reactions common to amino acids due to their α-carboxyl group.
  • •Explain reactions common to amino acids due to their α-amino group.
  • •Describe reactions specific to different functional groups in amino acid side chains.
  • •Understand the principles behind tests like Ninhydrin and Xanthoproteic reactions.
Week
5

Module 1: Amino Acids

2h

Unit 5: Ph, pk<sup>a</sup> and Buffering Capacity of Amino Acids

2 study hours
  • •Define pH and use its mathematical expression to perform calculations.
  • •Explain the dissociation of weak acids and its relation to pKa of amino acids.
  • •Define buffer solutions and describe their function.
  • •Solve problems using the Henderson-Hasselbalch equation.
Week
6

Module 2: Peptides

2h

Unit 1: Peptides-Formation and Nomenclature

2 study hours
  • •Define peptides and explain how they are formed.
  • •Describe the nature of the peptide bond.
  • •Explain how peptides are named.
  • •Understand the differences between peptides and proteins.
Week
7

Module 2: Peptides

2h

Unit 2: Properties, Examples and Functions of Biological Peptides

2 study hours
  • •State the properties of peptides.
  • •List some common biologically active peptides.
  • •Associate biological peptides with specific functions.
  • •Understand the ionic properties and titration curves of peptides.
Week
8

Module 2: Peptides

2h

Unit 3: Separation of Peptides I

2 study hours
  • •State the principles of peptide/protein purification.
  • •Explain how peptides are separated based on solubility.
  • •Explain peptide purification techniques based on molecular size.
  • •Understand techniques like dialysis, ultracentrifugation, and gel filtration.
Week
9

Module 2: Peptides

2h

Unit 4: Separation of Peptides II

2 study hours
  • •Differentiate between SDS-polyacrylamide gel electrophoresis and isoelectric focusing.
  • •Describe the procedure of affinity chromatography.
  • •Give examples of various ion-exchangers.
  • •Understand separation techniques based on charge and affinity.
Week
10

Module 2: Peptides

2h

Unit 5: Peptide Sequencing

2 study hours
  • •Outline the general steps for sequencing peptides and proteins.
  • •Describe the Edman degradation procedure.
  • •Understand the importance of preliminary steps in sequencing.
  • •Explain how to establish the overall sequence of a polypeptide.
Week
11

Module 3: Proteins

2h

Unit 1: Proteins nature, Properties, Examples and Biological Functions

2 study hours
  • •Describe the nature of proteins and their structural complexity.
  • •State some basic properties of proteins.
  • •Give examples of some proteins and their natural sources.
  • •Outline the functions of different proteins.
Week
12

Module 3: Proteins

2h

Unit 2: Structural Levels of Proteins

2 study hours
  • •Enumerate all the levels of protein structure.
  • •Define the primary structure of protein as an amino acid sequence.
  • •Describe the different conformations of the secondary structure of proteins.
  • •Explain the interactions of subunits of polypeptides in the quaternary level of protein structure.
Week
13

Module 3: Proteins

2h

Unit 3: Stability of Proteins –The Roles of Noncovalent Forces

2 study hours
  • •Explain the process of protein folding.
  • •Enumerate the noncovalent forces that participate in protein stability.
  • •Explain the nature of noncovalent forces.
  • •Explain how the compromise of these forces leads to denaturation of proteins' native conformations.

This study schedule is in beta and may not be accurate. Please use it as a guide and consult the course outline for the most accurate information.

Course PDF Material

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Study Tips & Exam Preparation

Expert tips to help you succeed in this course

1

Create flashcards for each amino acid, including its structure, properties, and classification.

2

Practice drawing peptide structures and naming them based on amino acid sequences.

3

Review the principles and applications of different protein purification techniques, such as gel filtration and affinity chromatography.

4

Understand the mechanisms of enzyme-catalyzed reactions and the factors affecting enzyme activity.

5

Focus on understanding the role of noncovalent forces in protein folding and stability.

6

Review the different levels of protein structure (primary, secondary, tertiary, and quaternary) and the bonds that stabilize them.

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