

Amino Acids & Protein
Presentation
•
Biology
•
11th - 12th Grade
•
Practice Problem
•
Easy
Gemma Quartermaine
Used 21+ times
FREE Resource
20 Slides • 9 Questions
1
Amino Acids & Protein
Advanced Animal Nutrition

2
Learning Objectives
Identify the difference between essential and non-essential amino acids
Explain the structure and features of amino acids and protein
Summarise the roles of protein
Simplify the process of how proteins are digested and absorbed
3
Open Ended
Provide a definition for an amino acid - be quick, you only have 3 minutes!
4
Amino Acids
Organic compounds containing amine and carboxyl functional groups, along with a side chain specific to each amino acid.
5
Amine group
6
Carboxyl group
7
Important of Amino Acids
Amino acids are the building blocks of Protein.
20% of the human body is made up of protein.
A large proportion of our cells, muscles and tissue is made up of amino acids, meaning they carry out many important bodily functions, such as giving cells their structure.
They also play a key role in the transport and the storage of nutrients.
8
Multiple Choice
Which sentence describes an essential amino acid?
These are amino acids that cannot be made by the body, so they are gained through food.
These are amino acids that can be produced by the body
9
Essential Amino Acids
Must be obtained through foods
Cannot be made by the body
9/20 are essential
Body does not store them, so must have daily supply
10
Non-Essential Amino Acids
Can be produced by the body
Not classed as essential, however fulfil essential roles in the body
When you’re sick or under significant stress, your body may not be able to produce enough of these amino acids to meet your needs
11
Amino Acids
The 9 essential amino acids are: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine.
The 11 nonessential amino acids: alanine, arginine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, proline, serine, and tyrosine.
12
Structure
All amino acids have a central carbon atom surrounded by a hydrogen atom, a carboxyl group, an amino group, and an R-group.
It is the R-group or side chain that differs between the 20 amino acids
Each amino acid has unique characteristics arising from the size, shape, solubility, and ionization properties of its R group.
13
Open Ended
Define a Zwitterion. You may use research to help you. You have 5 minutes for this task.
14
Amino Acids as a Zwitterion
Zwitterion = molecule or ion having separate positively and negatively charged groups.
An amino acid has both a basic amine group and an acidic carboxylic acid group
15
Amino Acids as a Zwitterion
Internal transfer of a hydrogen ion from the -COOH group to the -NH2 group
Leaving an ion with both a negative charge and a positive charge.
16
17
Task
Scan the QR code and watch the video.
The next set of questions are related to this video!
18
Open Ended
What is a polymer?
19
Open Ended
What is a monomer?
20
Open Ended
What is an alpha carbon?
21
Protein
Any of a class of nitrogenous organic compounds which have large molecules composed of one or more long chains of amino acids
22
Open Ended
Provide 5 examples of where protein can be sourced from.
23
Forming Proteins
Peptide bonds are formed by a biochemical reaction that extracts a water molecule as it joins the amino group of one amino acid to the carboxyl group of a neighbouring amino acid.
If proteins are being broken down - hydrolysis reaction
24
Primary Structure
Simplest level of protein structure
Refers to sequence of amino acids in polypeptide chain
Held together with peptide bonds
25
Secondary Structure
Secondary structure is local interactions between stretches of a polypeptide chain and includes α-helix and β-pleated sheet structures
Secondary structures arise as H bonds form between local groups of amino acids in a region of the polypeptide chain
26
Tertiary Structure
3-D shape formed through interactions within the polypeptide chain
Cysteine side chains form disulfide linkages in the presence of oxygen, the only covalent bond forming during protein folding
Hydrophobic R groups of nonpolar amino acids mostly lie in the interior of the protein, while the hydrophilic R groups lie mostly on the outside
27
Quaternary Structure
How its subunits are oriented and arranged with respect to one another.
Applies to multiple polypeptides proteins only
Any proteins with a single polypeptide will not have a quaternary structure
28
Open Ended
Research task: How is protein absorbed?
29
Open Ended
Research the functions of proteins - provide at least 4 functions of proteins in the body.
Amino Acids & Protein
Advanced Animal Nutrition

Show answer
Auto Play
Slide 1 / 29
SLIDE
Similar Resources on Wayground
21 questions
Best Method: Solving Systems of Equations
Presentation
•
7th - 10th Grade
21 questions
Cold War Intro
Presentation
•
KG
23 questions
APB - Unit 2 - Cell Structure and Function
Presentation
•
11th - 12th Grade
20 questions
How to Budget
Presentation
•
11th - 12th Grade
20 questions
The Nervous System
Presentation
•
11th - 12th Grade
25 questions
Probability of Simple Events
Presentation
•
11th - 12th Grade
22 questions
Endocrine system (Chapter 12) Biology F4 KSSM
Presentation
•
11th Grade
23 questions
Direct Object Pronouns
Presentation
•
11th - 12th Grade
Popular Resources on Wayground
10 questions
Main Idea and Supporting Details
Quiz
•
3rd - 6th Grade
20 questions
Math Review
Quiz
•
3rd Grade
14 questions
25-26 SY 8th Grade EOY Benchmark
Quiz
•
8th Grade
15 questions
Fast food
Quiz
•
7th Grade
20 questions
Math Review
Quiz
•
6th Grade
20 questions
Context Clues
Quiz
•
6th Grade
21 questions
EOY Grade 6 Benchmark Assessment - Content Skills
Quiz
•
6th Grade
20 questions
Inferences
Quiz
•
4th Grade