Mastering Amino Acids: Building Proteins for Biochemistry

Name: Mastering Amino Acids: Building Proteins for Biochemistry
Rating: 3.9 (12 reviews)

Unlock the Chemistry, Structure, and Functions of Amino Acids, peptides and Proteins

Created byDr. Rania S. Seoudi

Last updated 9/2023

English

English [Auto],

What you'll learn

Amino Acids, Peptides, and Protein Architecture
Chemistry
Biochemistry
Organic Chemistry
Peptide Synthesis
Protein Structure and Folding
Peptide Sequencing
Amino Acid Properties and Synthesis
Protein Interactions

Course content

5 sections • 18 lectures • 3h 13m total length

Introduction and Overview of Course Topics - Part 117:42
Explore amino acids, peptides, and proteins, alpha, beta, and gamma carbons, zwitterions, isoelectric points, and four synthesis methods: reductive amination, amination of alpha acids, Gabriel malonic ester synthesis, Strecker synthesis.
Introduction and Overview of Course Topics - Part 212:50
Explore amino acid chemistry, peptide and amide bonds, and how peptides become proteins, including alpha helix structures and beta sheets. Discover solid phase peptide synthesis to assemble peptides.
Lect.3_Amino Acids Structures and Conformations10:57
Explore amino acid structure and stereochemistry, from glycine to the common r-group variations, and learn to assign D/L and R/S configurations using Fischer projections and CIP priority.
Lect.4_Exercises on R and S16:29
Convert a sawhorse structure to a Fischer projection, assign the two chiral centers' R/S configurations, and review the 20 amino acids classified as nonpolar, polar, acidic, or basic.
Lect.5_Acid Base Behavior and pI10:41
Explore acid-base behavior of amino acids, formation of zwitterions, and how pKa values determine the isoelectric point, with examples like valine, serine, aspartic acid, and arginine.
Lect.6_Exercises on pI and Net Charge11:00
Explore how amino acid pKa values govern protonation states, calculate glycine, lysine, aspartic acid, and tyrosine charges across pH, and determine isoelectric points and zwitterion formation.

Synthesis of Amino Acids_Reductive Amination & SN2 reaction7:36
Explore amino acid synthesis methods, including reductive amination of alpha keto acids, sn2 reaction of alpha halo acids with ammonia, alkylation of diethyl malonate derivatives, and the strecker synthesis.
Synthesis of Amino Acids from Alkylation of a Diethyl Malonate Derivative9:16
Explore the mechanism of alkylating diethyl malonate derivatives to produce alpha amino acids, including hydrolysis, decarboxylation, and valine as the product.
Synthesis of Amino Acids Using Strecker Synthesis11:25
The Strecker synthesis converts an aldehyde to an amino acid through two stages: ammonia-mediated imine formation and hydrogen cyanide addition to form alpha-aminonitrile, then hydrolysis to alpha amino acid.

Separation of Amino Acids Treatment with Optically Pure Chiral Acid or Base16:10
convert racemic amino acids into diastereomers with optically pure chiral acid or base to enable separation by crystallization or chromatography; illustrate enzymatic resolution and acetylation with alpha methyl benzylamine.
Separation of Amino Acids Using Enzymatic Resolution6:11
Explain enzymatic resolution of amino acids, including acylase-selective hydrolysis of L amino acids, and enantioselective synthesis from achiral alkenes using chiral hydrogenation catalysts to yield single enantiomers.

Peptide Bond and Peptide Sequencing6:35
Explore how amino acids join via peptide bonds through a condensation reaction to form dipeptides, tripeptides, and proteins, covering amide bonds, n-terminal and c-terminal terminology, and peptide chain geometry.
Peptide Sequencing15:14
Identify amino acids by hydrolysis and chromatography, then sequence peptides using Edman degradation, phenyl isothiocyanate chemistry, and selective enzymatic hydrolysis (carboxypeptidase, chymotrypsin, trypsin) to reveal order.
Peptide Synthesis8:14
Peptide synthesis protects amino and carboxyl groups to direct condensation, using DCC activation to form dipeptides such as alanine glycine with water removal.
Automated Peptide Synthesis (Merrifield Method)4:36
Learn automated peptide synthesis via the Merrifield solid-phase method, using polystyrene on a solid support, fmoc protection, piperidine deprotection, and DCC activation to build peptides efficiently, reducing time and cost.

Protein Structure and Interactions13:51
Explore how amino acids link via peptide bonds to form polypeptide chains, whose primary structure and hydrogen bonds drive folding into alpha helices, beta sheets, and functional interactions.
Protein Tertiary Structure and Interactions7:42
Explore how proteins fold from secondary to tertiary structures, stabilized by non-covalent hydrophobic interactions, hydrogen bonds, electrostatic interactions, and disulfide covalent bonds, forming fibrous and globular shapes and quaternary complexes.
Summay and Conclusion6:36
Explore amino acids, peptides, and proteins, including alpha amino acids, their side chains, isoelectric points, peptide bonds, and protein folding into secondary and quaternary structures.

Requirements

No requirements

Description

This course explore the structure, synthesis, and chemistry of these essential building blocks of life. In this comprehensive course, you will explore biomolecules' structure, synthesis, and chemistry.

The primary topics covered in this course are:

1. Amino Acid Synthesis structure and chemistry: The various methods and mechanisms involved in amino acid synthesis. Learn about the different pathways and reactions required to create these fundamental protein building blocks. Understand the importance of stereochemistry in amino acid synthesis.

You will explore the structural features of amino acids, including their backbone, side chains, and functional groups. Gain insight into amino acids' physicochemical properties, such as acidity and basicity. Study the reactivity of amino acids, including their involvement in peptide bond formation and other chemical reactions.

2. Peptides and Polypeptides: Investigate the formation and properties of peptides and polypeptides. Understand how amino acids are linked together through peptide bonds to form these chains. Explore the different types of peptides, including dipeptides, tripeptides, and longer polypeptide chains, and how to separate them. Explain the principles behind these techniques and their application in peptide analysis and sequencing.

3. Protein Structures: Examine the hierarchical levels of protein structure, including primary, secondary, tertiary, and quaternary structures. Understand how the sequence of amino acids determines the folding and conformation of proteins. Explore the forces and interactions that stabilize protein structures and contribute to their unique functions.

By the end of this course, you will have a deep understanding of amino acids, peptides, and protein chemistry. You will be equipped with the knowledge and tools to analyze, synthesize, and comprehend biomolecules. Join us on this exciting journey and unlock the secrets of amino acids, peptides, and proteins!

Who this course is for:

Biochemistry
Students
Chemistry
Medicine
Pharmacy
Undergratue
Collage Students
University Students

Mastering Amino Acids: Building Proteins for Biochemistry

What you'll learn

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Course content

Introduction6 lectures • 1hr 20min

Amino Acids Synthesis3 lectures • 28min

Separation of amino acids2 lectures • 22min

Peptides and Proteins4 lectures • 35min

Protein Primary and Secondary Structures3 lectures • 28min

Requirements

Description

Who this course is for: