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Amino Acids & Protein

Amino Acids & Protein

Assessment

Presentation

Biology

11th - 12th Grade

Practice Problem

Easy

Created by

Gemma Quartermaine

Used 21+ times

FREE Resource

20 Slides • 9 Questions

1

Amino Acids & Protein

Advanced Animal Nutrition

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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

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Open Ended

Provide a definition for an amino acid - be quick, you only have 3 minutes!

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Amino Acids

  • Organic compounds containing amine and carboxyl functional groups, along with a side chain specific to each amino acid.

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Amine group

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Carboxyl group

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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?

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These are amino acids that cannot be made by the body, so they are gained through food.

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These are amino acids that can be produced by the body

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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

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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

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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.

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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 sizeshapesolubility, and ionization properties of its R group.

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13

Open Ended

Define a Zwitterion. You may use research to help you. You have 5 minutes for this task.

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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

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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.

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Task

Scan the QR code and watch the video.

The next set of questions are related to this video!

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18

Open Ended

What is a polymer?

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Open Ended

What is a monomer?

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Open Ended

What is an alpha carbon?

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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.

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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

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Primary Structure

  • Simplest level of protein structure

  • Refers to sequence of amino acids in polypeptide chain

  • Held together with peptide bonds

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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

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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

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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

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28

Open Ended

Research task: How is protein absorbed?

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Open Ended

Research the functions of proteins - provide at least 4 functions of proteins in the body.

Amino Acids & Protein

Advanced Animal Nutrition

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