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54 Cards in this Set

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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
Active site
the portion of the enzyme where bonds are made or broken
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