Grade 10 - Biology - LO.5 - Proteins in cells

We have in LO.5 Biology G10

First: the Concepts

Functions of Proteins in cells

a. Proteins in cells

b. Protein classification

c. Enzyme structure, functions and factors affecting rates.

Second: the References

Cell Biology- Unit 3 - Act.10 Functions of Proteins in Cells(Teacher .SEPUP 330-338 - S.SEPUP 213 215) 

Unit 3 - Act 10 - TR 10.1; SS 10.1

Cell Biology- Unit 3 - Act.11 Investigating Enzyme Function (Teacher .SEPUP 339-346 -S.SEPUP 216-218)

Unit 3- Act 11 - TR 11.1

Campbell: chapter 5.4

Third: the Videos links

Fourth: Skills

Correlate (identify the relationship between) structure

and function.

Fifth: the materials as PPT., DOCX., and PDF

In the Drive from this link

Few Notes:

Polypeptides are polymers built from the same set of 20 amino acids

A protein consists of one or more polypeptides

Amino acids are organic molecules with carboxyl and amino groups

Amino acids differ in their properties due to differing side chains, called R groups

Amino acids are linked by peptide bonds

A polypeptide is a polymer of amino acids

Polypeptides range in length from a few to more than a thousand monomers 

Each polypeptide has a unique linear sequence of amino acids

A functional protein consists of one or more polypeptides twisted, folded, and coiled into a unique shape

The sequence of amino acids determines a protein’s three-dimensional structure

A protein’s structure determines its function

Four Levels of Protein Structure:

The primary structure of a protein is its unique sequence of amino acids

Secondary structure, found in most proteins, consists of coils and folds in the polypeptide chain

Tertiary structure is determined by interactions among various side chains (R groups)

Quaternary structure results when a protein consists of multiple polypeptide chains

Primary structure, the sequence of amino acids in a protein, is like the order of letters in a long word 

Primary structure is determined by inherited genetic information

The coils and folds of secondary structure result from hydrogen bonds between repeating constituents of the polypeptide backbone

Typical secondary structures are a coil called an α helix and a folded structure called a β pleated sheet

Tertiary structure is determined by interactions between R groups, rather than interactions between backbone constituents

These interactions between R groups include hydrogen bonds, ionic bonds, hydrophobic interactions, and van der Waals interactions

Strong covalent bonds called disulfide bridges may reinforce the protein’s structure

Quaternary structure results when two or more polypeptide chains form one macromolecule

Collagen is a fibrous protein consisting of three polypeptides coiled like a rope

Hemoglobin is a globular protein consisting of four polypeptides: two alpha and two beta chains

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