PPT-Proteins: Secondary

and Tertiary Structure Need TO Book Plasticene OHP OHT OHT pens Textbooks Repro Sources Flipped learning task in folder lesson 8 to set as homework Success Criteria Know about protein structure. Why do we want to know protein structure?. Classification. Functional Prediction. What is protein structure?. Primary - chains of amino acids. Secondary - interaction between groups of amino acids. Tertiary - the organization in three dimensions of all the atoms in a polypeptide. E – Recall the different structures of proteins and the test for proteins..  . C. . – Describe how a peptide bond is formed. . Describe the different structure of proteins.  . A – . Explain how the structures of a polypeptide build up and how changes to this may affect function. The 411. Proteins account for more than 50% of the dry mass of most cells. Protein functions include structural support, storage, transport, cellular communications, movement, and defense against foreign substances. PROTEINS – (DR. TRAISH) Introduction to Proteins - Proteins are abundant and functionally diverse molecules - They participate in cell regulation at all levels - They share a common structural Proteins. The Role of Enzymes. Success criteria. By the end of this lesson we will be able to:. State what elements are found in proteins. Describe what is meant by primary, secondary and tertiary structure of proteins.. Introducing proteins. Proteins. are a diverse group of large and complex polymer molecules, made up of long chains of . amino acids. .. They have a wide range of biological roles, including:. structural:. Most abundant molecule in cells making up 50% or more of their dry weight. Every protein has a unique structure, or shape. Allows it to perform a specific function. Enzymes are proteins that function as catalysts for many reactions in foods. strech. of the polypeptide chain. 5.4 Å rise,. 3.6 . aa. /turn.  1.5 . Å/. aa. N-term. C-term. prototypical .  = -57. ψ. . = -47. α-Helices have a dipole moment, due to . unbonded. and aligned N-H and C=O groups. Dr. . Shaimaa. . Munther. . Learning Outcomes - Proteins. Define the levels of protein conformation and to indicate the role of weak interactions.. Illustrate how protein structure relates to protein function using examples.. Dr. Ahmed Mujamammi. Dr. . Sumbul. . Fatma. Learning outcomes. What are proteins?. Structure of proteins:. Primary structure.. Secondary structure.. Tertiary structure.. Quaternary structure.. Denaturation of proteins.. Proteins are biopolymers, made of the 20 L- . α. -amino acids linked by peptide bonds.. Polypeptide backbone is a repeating sequence of. . N-C-C-N-C-C…. The side chain or R group is not a part of the backbone or the peptide bond.. A. . Peptides. are compounds, formed of less . than . 50 . amino acids . linked together by peptide bonds.. 1.. . Dipeptide. (2 amino acids and one peptide bond).. 2.. . Tripeptide. (3 amino acids and two peptide bonds).. Some of the slides are adapted from Dr. Dong Xu’s lecture notes. Why secondary structure prediction?. Accurate secondary structure prediction can be an important information for the tertiary structure prediction. Unit 1 Advanced Higher. Miss Aitken. Pages 16-25. Textbook. Proteomics. Genome:. complete set of DNA. Comprises of coding and non-coding areas. 20-25000 genes in human genome. Proteome:. Entire set of proteins that can be expressed from a genome.