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Understanding Protein Structures: Formation, Functions, and Denaturation

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8 diapositives · 298 Views · Aug 06, 2014

This lesson delves into the fundamental structures of proteins, which are vital macromolecules in biological systems. Proteins are made from chains of 20 different amino acids, and their unique sequences determine their structure and function. We explore the four levels of protein structure: primary (linear), secondary (α-helix and β-sheets), tertiary (3D shape), and quaternary (multiple polypeptides). Additionally, we discuss how environmental factors like temperature and pH can lead to denaturation, making proteins biologically inactive, and highlight the implications of these changes in enzymatic activity.

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  1. C-Notes: Proteins General Structure Stnd: BI.5a 9/16/13 SWBAT identify proteins general structures and functions in cells. Objective:

  2. What are the structures of proteins? • Proteins are made of chains of AMINO ACIDS. • There are only 20 amino acids andcan be combined in nearly countless ways. • The sequence of amino acids determines the shape of the protein. The shape of the protein is the biggest factor that determines its function. • There are 4 levels of structure • Primary structure • Linear shape (straight line) • Secondary structure (2 types) • Folding of protein structure • -helix (spiral shape) and -sheets (folded shape) • Tertiary structure • actual 3D shape • Quaternary structure • When 2 or more smaller polypeptides w/ different shapes join together. • Any alteration in the structure or sequencing changes the shape and function of the protein

  3. Secondary Protein Structure Amino acid subunits b pleated sheet Amino acid subunits  helix b pleated sheet  helix

  4. Polypeptide chain b Chains LE 5-20e Iron Heme a Chains Hemoglobin Polypeptide chain Collagen

  5. Because proteins shape are affected by temperature and pH changes. • It loses its normal shape when it is not in ideal optimal environmental conditions. • When a protein loses its normal shape, this is called denaturing. • A denatured protein is biologically INACTIVE. • Denaturing is usually permanent and not reversible. What happens when enzymes (proteins) Denature?

  6. Denaturing a Protein Figure 6.5

  7. SHAPE! For enzymes…What matters?

  8. Structural Differences Between Carbohydrates, Lipids, and Proteins Figure 6.1