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BCH210H1 Study Guide - Comprehensive Final Exam Guide - Protein, Protein Structure, Alpha Helix


Department
Biochemistry
Course Code
BCH210H1
Professor
Wright
Study Guide
Final

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BCH210H1

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BCH210 - Lecture 1
Red Blood cells
Hemoglobin
Protein
Red colour cause by the Fe heme complex
Tetramer: 2 alpha and two beta polypeptide chains
Sickle Cell Anemia
Signal change in amino acid (beta change)
Caused by the replacement of the beta subunit from Val to Glu
Hemoglobin S (Hb S) forms a long forms a long polymer → changes the RBC’s shape
Proteins
Polymers of amino acids
Amino acids linked by peptide bonds
Amino acids determine the structure of the protein folding
Key to biological functions → work as enzymes
Encoded by genes → mutation in genes causes mutated protein → lead to diseases
Molecules of Life
Proteins
Water
Ions
Vitamins
Sugar
Lipids
DNA & RNA
H2O
Polar
Important solvent & reactant biological reaction
Many protein are water soluble
Responsible for molecular structure
Certain enzymes and structure are produced in water
Forces
Hydrophobic (scared of water)
Ionic interactions (opposite charges)
Hydrogen bonds (specific - based in DNA use H bonds)
Van der Waals (contact)
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Hydrophobic effect
Effects the shape of the protein structure
H2O as a solvent
Hydrophobic (non polar) amino acids would be interior part of the globular protein
Hydrophilic (polar) amino acid would be on the exterior part of the globular
protein
ATP
Contains:
Tri phosphate group
Sugar ribose
Adenine base
C and N bond between the base and ribose
produces a nucleoside (adenosine)
Metabolism is required a person to make and use ATP at their own weight
NADPH
Starts off as ATP
Has nicotinamide
ATP production pathway
Best source of production for ATP: carbohydrates (SUGAR)
Glucose enters the pathway at the very beginning while fats and protein can enter later
on in the cycle
Draw the ATP cycle
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