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BIO213Sciences2 Unitsintermediate

General Biochemistry I

This course, General Biochemistry I, delves into 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 covers amino acid classifications, properties, reactions, peptide formation, separation techniques, and protein structure levels. It aims to develop a comprehensive understanding of how biomolecule structures influence cellular functions, providing a foundation for further studies in biochemistry and related fields.

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52h
Study Time
13
Weeks
4h
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
Theoretical Focus

Course Topics

Key areas covered in this course

1

Amino Acids

2

Peptides

3

Proteins

4

Enzymes

5

Protein Structure

6

Protein Stability

Total Topics6 topics

Requirements

Knowledge and skills recommended for success

Basic knowledge of biology and chemistry

💡 Don't have all requirements? Don't worry! Many students successfully complete this course with basic preparation and dedication.

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 ScienceHealthcareResearch

Study Schedule Beta

A structured 13-week journey through the course content

Week
1

Module 1: Amino Acids

4h

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.
  • •Describe the basic structure of amino acids, including the naming of carbon atoms and chirality.
  • •Write the structures of common amino acids like Glycine, Alanine, and Serine.

Unit 2: Classification of Amino Acids

2 study hours
  • •Classify amino acids based on their structures, polarity, and nutritional requirements.
  • •Identify and describe the structures of all common amino acids.
  • •Distinguish between polar and nonpolar amino acids.
  • •Explain the difference between essential and non-essential amino acids.
Week
2

Module 1: Amino Acids

4h

Unit 3: Properties of Amino Acids

2 study hours
  • •Discuss the physical properties of amino acids, including their response to heat and solubility.
  • •Explain the optical activity of amino acids and their absorption of light.
  • •Describe the acid-base properties of amino acids and their behavior in solution.
  • •Interpret the titration curve of simple amino acids and understand the concept of isoelectric point.

Unit 4: Chemical Reactions of Amino Acids

2 study hours
  • •Describe the reactions of α-carboxyl and α-amino groups in amino acids.
  • •Explain specific reactions for different functional groups in amino acid side chains.
  • •Discuss reactions such as disulfide bond formation, xanthoproteic reactions, and Sakaguchi reaction.
  • •Understand the application of these reactions in identifying and quantifying amino acids.
Week
3

Module 1: Amino Acids

3h

Unit 5: Ph, Pka and Buffering Capacity of Amino Acids

3 study hours
  • •Define pH and use its mathematical expression to perform calculations.
  • •Explain the dissociation of weak acids and the concept of pKa.
  • •Define buffer solutions and describe how they maintain pH.
  • •Solve problems using the Henderson-Hasselbalch equation.
  • •Understand the role of amino acids as biological buffers.
Week
4

Module 2: Peptides

4h

Unit 1: Peptides-Formation and Nomenclature

2 study hours
  • •Define peptide and explain how peptides are formed through peptide bonds.
  • •Describe the nature of the peptide bond and its properties.
  • •Explain how peptides are named according to their amino acid residues.
  • •Differentiate between peptides and proteins based on molecular weight.

Unit 2: Properties, Examples and Functions Of Biological Peptides

2 study hours
  • •State the properties of peptides, including their ionic and acid-base characteristics.
  • •List common biologically active peptides and associate them with their specific functions.
  • •Explain the titration curves and isoelectric points of peptides.
  • •Provide examples of biological peptides such as glutathione, oxytocin, and glucagon.
Week
5

Module 2: Peptides

3h

Unit 3: Separation of Peptides I

3 study hours
  • •State the principles of peptide/protein purification.
  • •Explain how peptides are separated based on solubility using salting out techniques.
  • •Describe peptide purification techniques based on molecular size, including dialysis, ultracentrifugation, and gel filtration.
  • •Understand the preliminary steps to peptide purification, such as cell disruption and centrifugation.
Week
6

Module 2: Peptides

3h

Unit 4: Separation of Peptides II

3 study hours
  • •Define terms like electrophoretic mobility and isoelectric pH in relation to protein separation.
  • •Differentiate between SDS-polyacrylamide gel electrophoresis and isoelectric focusing.
  • •Describe the procedure of affinity chromatography.
  • •Give examples of various ion exchangers and explain their use in ion exchange chromatography.
Week
7

Module 2: Peptides

3h

Unit 5: Peptide Sequencing

3 study hours
  • •Outline the general steps for sequencing peptides and proteins.
  • •Describe the preliminary steps to sequencing, including establishing the number of polypeptide chains and cleaving disulfide bridges.
  • •Explain the Edman degradation procedure and its importance in determining amino acid sequences.
  • •Discuss the methods for separating and purifying small peptides for sequencing.
Week
8

Module 3: Proteins

3h

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

3 study hours
  • •Describe the nature of proteins as polymers of amino acids.
  • •State the basic properties of proteins, including molecular weight, UV absorption, and charge.
  • •Give examples of proteins such as hemoglobin, albumin, and keratin.
  • •Outline the biological functions of different proteins, including transport, structural support, and catalysis.
Week
9

Module 3: Proteins

3h

Unit 2: Structural Levels of Proteins

3 study hours
  • •Enumerate all the levels of protein structure: primary, secondary, tertiary, and quaternary.
  • •Define the primary structure of a protein as its amino acid sequence.
  • •Describe the different conformations of secondary structure, including α-helix and β-conformation.
  • •Explain the three-dimensional arrangement of atoms in protein tertiary structure.
  • •Discuss the interactions of subunits of polypeptides in quaternary structure.
Week
10

Module 3: Proteins

3h

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

3 study hours
  • •Explain the process of protein folding and the role of molecular chaperones.
  • •Enumerate the noncovalent forces that participate in protein stability: hydrophobic interaction, hydrogen bonding, electrostatic forces, and van der Waals forces.
  • •Explain how the compromise of these forces leads to denaturation of proteins' native conformations.
  • •Describe the effects of denaturing agents such as heat, pH changes, detergents, and organic solvents.
Week
11

Module 3: Proteins

3h

Unit 4: Classification of Proteins

3 study hours
  • •Discuss the criteria for classifying proteins: biological functions, structural complexity, and shape.
  • •List the major functional classes of proteins and give their biological functions: catalytic, transport, structural, regulatory, storage, scaffold, and protective.
  • •Differentiate between simple and conjugated proteins.
  • •Give examples of globular and fibrous proteins.
Week
12

Module 3: Proteins

3h

Unit 5: Enzymes, Co-Enzymes and Vitamins

3 study hours
  • •Define enzymes and name some examples.
  • •Mention the major classes of enzymes and their functions.
  • •Outline the key properties of enzymes, including their catalytic power, specificity, and sensitivity to temperature and pH.
  • •Explain how enzymes perform their work by lowering activation energy and forming enzyme-substrate complexes.
  • •Differentiate the roles of co-enzymes, co-factors, and vitamins in relation to enzyme activity.
Week
13

Course Review

4h

Final Revision

4 study hours
  • •Review all modules and units.
  • •Focus on key concepts and definitions.
  • •Complete any outstanding assignments.
  • •Prepare for final examinations.

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

Read the complete course material as provided by NOUN.

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Study Tips & Exam Preparation

Expert tips to help you succeed in this course

1

Create concept maps linking amino acid structures to their properties (Units 1-3).

2

Practice drawing peptide structures and naming conventions (Module 2).

3

Review separation techniques and their applications (Module 2, Units 3-4).

4

Focus on understanding the forces stabilizing protein structure (Module 3, Unit 3).

5

Memorize key enzyme classifications and examples (Module 3, Unit 5).

6

Review all tutor-marked assignments and self-assessment questions.

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