Organic Chem Proteins-Carbs
Terms
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- Lipids
- Biochemical amenable to extraction w/a non-polar solvent
- Non-saponifiable lipids
- steroids, terpenes, prostaglandins
- steroids
- non-aromatic 4-ring structure
- terpenes
- hydrocarbon based on "isoprene" 10,15,20,25 carbons
- Fatty acids
- long chain carboxlyic acid that can be saturated or unsaturated
- Natural oils & fats
- are "mixtures" of many different tryglycerides
- Detergents
-
cleansing agents that are synthetic
-all amphipathic - Iodine
- the # of grams of I2(s) that will add to the double bonds in 100g of the oil or fat
- Phospholipids
- Make up the membranes of cells
- Plasmologens
- Glycerol-based phospholipids w/an unsaturated ether group
- Glycolipid
- Sphingosine-based lipid w/a sugar unit
- Proteins
-
Amino acid-based macro molecules
-most abundant biological molecule in body - Essential Amino Acids
- One that the body can't synthesize in high enough concentration for growth
- Perfect or complete protein
-
Will contain all of the essential amino acids
ex. beans + rice= perfect protein - Isoelectric point
- The pH at which an amino acid exists in its neutral Zwitterion form.
- Protein primary structure
- the sequence of amino acids in a protein chain that determines the shape of the protein
- Protein secondary structure
- held together to another protein strand by H bonds on main chain creating a beta-pleated sheet, alpha-helix, triple helix, random coil
- Tertiary structure
- the 3D shape that secondary structure assumes w/from 4 types of interactions (mostly side chains)
- Quaternary structure
- joining together of tertiary sub-units into the final native confirmation, which is the shape of a working protein
-
Alpha-helix
-secondary structure -
-flexible & elastic
-alpha-keratin
-wool, fingernails -
B-pleated sheet
-secondary structure -
-one strand to another, parallel fashion
-side/side strands
-beta keratin
-bloodclots
-flexible w/some elasticity -
Triple helix
-secondary structure -
-very hard to digest
-unusually strong
-collagen fibrils
-bones are made out of triple helix -
Random coil
-secondary structure - -3D shape from H bond of main chain with side chain
- Disulfide bonds
- comes from the oxidatin of 2 cysteines* 10x as strong as other 3 bonds (H, salt bridge, hydrophobic interaction
- Alpha helix
-
confirmation held togehter by hydrogen bonds on main chain of one strand about itself
-3.6 amino acids per turn - Protein function
- what proteins do in the body
- Denaturation of protein
-
A destruction or alteration of "Native conformation"
-Occurs at the tert. level - Denaturation types
- heat, alcohols, organic solvents, acids/bases, oxidation & reduction, metal ions, violent agitation
- Protein properties
- Denaturation, Tindall effect, Hydrolysis
- General protein types
- fibrous & globular
- Fibrous protein
-
-indigestible
-triple helix
-very strong= bones - Globular protein
-
-digestible
-random coil
-tightly folded strands to form unique shape - Enzymes
- Biological catalysts
- Catalyst
- Changes the velocity of a reaction & alters the mechanism. Lowers the energy of activation "collision theory"
- Some functions of proteins
-
Motility Actin & myosin
Storage ferratin
hormoneschem. messengers
enzymesbiological catalysts - Enzyme
- A protein or other molecule that acts as a catalyst for a biological reaction.
- Apoenzyme
- protein part of the enzyme
- Activity
- how efficient the enzyme is
- Active site
- the portion of the enzyme where bonds are made or broken
- Substrate
- molecule that enzyme acts on
- coenzymes
-
usually amines w/carbon ring system
-"the vital amines" vitamines - cofactor
-
the non-protein portion of the enzyme
-often contains a metal
AKA Prosthetic group - Prosthetic group
- a helper part of the enzyme- non protein organic portion
- Induced fit
- substrate will "construct" the enzyme or the presence of the substrate causes enzymes to come & match it.
- How do you regulate enzymes?
-
1) Inhibition by a competitor at active site.
2)Limit substrate by compartmentalization
3)Control of synthesis of substrate - Metabolism
- the net sum of reactions in the body
- Catabolism
-
breaking down of lrg. biomolecules into smaller ones
-processoxidation reaction
-YIELDS energy - Anabolism
-
the building up of larger biomolecules from smaller precursors
-this process USES energy - Basal metabolism
- The energy turnover in the basal state (total rest) is about 1/2 energy
- Basal metabolic rate
- The rate of O2 uptake in the basal state
- Energy equivalents of food
-
Lipids 9.5 Kcal/gm
Alcohol ethanol 7.1 Kcal/gm
Proteins 4.3 Kcal/gm
Carbs 4.2 Kcal/gm - Best approach fro weightloss
- Calorie deficit PLUS high rate of activity
- Ways to increase BMR
-
1) Exercise
2) Exposure to cold
3) anxiety, worry, insomnia