Protein Structure and Function

Note Packet

Lesson Topic Statement(s) and Objective(s) Activities
1 Amino Acids

2.1.S1:  Drawing molecular diagrams of glucose, ribose, a saturated fatty acid and a generalized amino acid.

  • Draw the generalized structure of an amino acid.

  • Label the amine group, carboxyl group, alpha carbon and R group on an amino acid.


2.4.U2: There are 20 different amino acids in polypeptides synthesized on ribosomes.

  • State the number of amino acids used by living organisms to make polypeptides.

  • Given an image of an amino acid, classify the amino acid chemical properties based on R group properties. 


2.4.NOS:  Looking for patterns, trends, and discrepancies- most but not all organisms assemble proteins from the same amino acids.

  • Explain the trend of organisms assembling polypeptides from the same amino acids.

  • Describe a discrepancy of the trend of all organisms using the same amino acids to assemble polypeptides.

Where are we now slide

Amino acid notes

Amino acid cards

Amino acids properties handwritten 

Amino acids properties list

Amino acid handwritten notes

A&B:  Evolutionary History of Amino Acids
2 Essential Amino Acids

D.1.U4:  Some fatty acids and some amino acids are essential.

  • Outline the concept of “conditionally essential” using amino acid examples.


D.1.U1:  Essential nutrients cannot be synthesized by the body, therefore they have to be included in the diet.

  • Define “essential” as related to dietary nutrients.

  • Define “non-essential” as related to dietary nutrients.


D.1.U5:  Lack of essential amino acids affects the production of proteins.

  • Outline the effect of protein deficiency malnutrition on children and adults.

Essential Amino Acids notes

Essential amino acids for humans chart

3 Protein Folding

7.3.U7:  The sequence and number of amino acids in the polypeptide is the primary structure.

  • Describe the primary structure of a protein, including the type of bonding involved.


2.4.U4:  The amino acid sequence of polypeptides is coded for by genes.

  • Outline the relationship between genes and polypeptides.


2.4.U1:  Amino acids are linked together by condensation to form polypeptides.

  • Describe polypeptide chain formation in terms of the formation of peptide bonds and condensation reactions.

  • Determine the number of peptide bonds given the number of amino acids in a polypeptide.

  • Define dipeptide, oligopeptides and polypeptide.  


2.4.S1:  Drawing molecular diagrams to show the formation of a peptide bond.

  • Draw peptide bond formation in condensation reactions.


2.4.U3:  Amino Acids can be linked together in any sequence giving a huge range of possible polypeptides.

  • Calculate the possible number of amino acid sequences given n number of amino acids.


7.3.U8:  The secondary structure is the formation of alpha helices and beta pleated sheets stabilized by hydrogen bonding

  • Describe the secondary structure of a protein, including the type of bonding involved.

  • Identify the alpha-helix and beta-pleated sheet in images of protein structure.


7.3.U9:  The tertiary structure is the further folding of the polypeptide stabilized by interactions between R groups.

  • Describe the tertiary structure of a protein, including the types of R group interactions involved.

  • Explain how the chemical characteristics of R groups in the polypeptide chain affect protein folding.


2.4.U6:  The amino acid sequence determines the three-dimensional conformation of a protein.

  • Contrast the structure of globular proteins with the structure of fibrous proteins.

  • Describe the structure of membrane bound globular proteins.


2.4.U5:  A protein may consist of a single polypeptide or more than one polypeptide linked together.

  • Outline the structure and function of three example proteins composed of two or more polypeptides linked together.


7.3.10:  The quaternary structure exists in proteins with more than one polypeptide chain (may also involve the binding of a prosthetic group to form a conjugated protein).

  • Outline the quaternary structure of protein folding.

  • Describe the structure of a conjugated protein, including the  prosthetic group.

Protein folding slides

Protein folding dance and example

Handwritten protein folding notes

Handwritten protein folding review

Vision learning proteins

Scitable:  protein structure

NCBI reading

Proteins - Pathway - LabXchange

Reading:  3D structure of protein

Reading:  Alzheimer’s prion

Reading:  mystery of protein folding

Reading:  proteins and proteomics

Reading:  seeds of dementia

Reading: when good proteins go bad

Reading:  seeds of dementia

Scitable:  the protein data bank

Sctable:  protein folding and disease

Modeling dipeptide formation

Protein folding toobers

DNA sequences for toobers

Amino acid side chains for toobers

Toobers lab scoring sheet

Insulin folding model

Protein folding with beads

Modeling protein folding with paper amino acids

Jolecule visualization (DK)

Protein molecular visualization

Protein folding simulation

Huntington's spreads like 'fire in the brain.' Scientists say they've found the spark

Course Source - CoV Spike Protein Visualization

Course Source - Gluten Protein

Rational drug design lesson

A&B:  Biochemistry: Peptide 'fingerprint' enables earlier diagnosis of Alzheimer's disease 

A&B:  ‘The entire protein universe’: AI predicts shape of nearly every known protein
4 Denaturation  

Denaturation notes

Denaturation handwritten 

Albumin Denaturation lab

Protein Eggsperiment

Egg Cooking Scale

Eggsperiment Data Collection Form

Eggsperiment scoring sheet

A&B:  renaturing egg proteins
5 Protein Functions

2.4.U8:  Every individual has a unique proteome .

  • Define proteome.

  • Contrast proteome with genome.


2.4.U7:  Living organisms synthesize many different proteins with a wide range of functions.

  • Contrast the generalized function of globular proteins with generalized function of fibrous proteins.

  • List nine functions of proteins in a cell or organism.

  • Describe the function of enzyme proteins.

  • Describe the function of hormone proteins.

  • Describe the function of immunoglobulin proteins.

  • Describe the function of pigment proteins.

  • Describe the function of structural proteins.


2.4.A1:  Rubisco, insulin, immunoglobulins, rhodopsin, collagen and spider silk as examples of the range of protein functions.

  • State the function of each of the following proteins:

    • rubisco

    • insulin

    • immunoglobulin

    • rhodopsin

    • collagen

    • spider silk

    • actin

    • myosin

    • casein

    • hemoglobin

    • acetylcholine receptor

    • oxytocin

    • prolactin

    • ferritin

    • bilirubin

    • fibrinogen

    • transferrin

    • albumin

Intro to the Proteome notes

Protein function notes

Classes of proteins handwritten notes

Scitable:  protein function

Protein structure/function jigsaw slides

Protein structure/function sorting cards

Protein structure/function Jamboard sort

Protein “speed dating”

A&B:  Proteins rule (questions)

A&B:   tangled protein web

A&B: Spider Silk Is Stronger Than Steel. It Also Assembles Itself.
6 Wrap Up and Review  

Final knowledge audit

1-pager

Self-quiz

Review slides

Kahoot review 1

Kahoot review 2

Kahoot review 3

Kahoot review 4

Kahoot review 5

Quizizz Review 1

Quizizz Review 2