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65 Cards in this Set
- Front
- Back
biochemistry
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study of chemical composition and reactions of living matter
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organic compounds
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-contain carbon
-covalently bonded molecules -many large -includes proteins, carbs, lipids (fats), nucleic acids |
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inorganic compounds
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-don't contain carbon
-include water, salts, acids, bases |
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water
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-most abundant inorganic compound
60%-80% of volume |
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water properties
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1) high heat capacity
2) high heat of vaporization 3) polar solvent properties 4) reactivity 5) cushioning |
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water: high heat capacity
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-absorbs & release large amounts of heat
-prevents changes in temp. (homeostasis)- water redistributes heat |
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water: high heat of vaporization
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-changes form liquid to gas
-heat absorbed breaks H bonds -sweat- heat removed from body providing cooling mechanism |
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water: polar solvent properties
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water- universal solvent
polarity- water molec. moves from neg. ends toward pos. ends -explains how compounds dissociate -forms hydration layers |
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water as an excellent solvent
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nutrients, resp. gases, metabolic wastes carried throughout body- dissolved in blood plasma & metabolic wastes excreted from urine
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water: reactivity
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-most important reactant
hydrolysis- add water to break bond dehydration- water molec. is removed to form bond |
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water: cushioning
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-form resilient cushion around certain body organs
-helps protect from physical trauma |
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salts
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-ionic compound containing cations other than H+ and anions other than hydrodxyl ion OH-
-inorganic, dissolves in water -expl: NaCl, CaCo3, KCl |
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electrolytes
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substances that conduct electrical current
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acids
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-have sour taste
-react w/ metals, burn "hole" -release hydrogen ions (H+) -proton donors -concent. of H+ determines acidity |
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bases
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-have bitter taste
-feel slippery -release hydroxyl ions (OH-) & take up H+ -proton acceptors expl: bicarbonate ion (HCO3-) ammonia (NH3) |
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pH: Acid-Base Concentration
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-based on concentration of hydrogen ions
-more H+, more acidic -more OH-, more basic runs from 0-14 pH: 7.00 neutral pH: 0-6.99 acidic pH 7.01-14 basic |
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neutralization
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-joins H+ or OH- to form water and neutralizes solution
-acids & bases mixed, forms water and salt |
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buffers
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-resist abrupt and large swings in pH of body fluids
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strong acids
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-dissociate completely & irreversibly in water
-can dramatically change pH |
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weak acids
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don't dissociate completely
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strong base
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dissociate easily in water & quickly join with H+
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weak base
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ionizes incompletely and reversibly
expl: bicarbonate ion |
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carbonic acid-bicarbonate system
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-carbonic acid dissociates reversibly
-release bicarbonate ions & protons -chem. equilibrium between carbonic acid (weak acid) & bicarbonate ion (weak base) resists changes in blood pH |
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carbon is electroneutral
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-never loses or gains electrons
-always shares electrons |
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carbohydrates
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-group of molecules that includes sugars and starches
contain C, H, O classified according to size/solubility |
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monosaccharides
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structural units or building blocks of carbohydrates
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monosaccharides
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-simple sugars
-single-chain or single-ring structures -contain 3 to 7 carbon atoms -C, H, O |
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disaccharides
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-double sugars
-two monosaccharides joined by dehydration synthesis expl: glucose+fructose=sucrose glucose+galactose=lactose glucose+glucose=maltose |
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polysaccharides
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-long chains of simple sugar
-linked by dehydration synthesis -units: polymers -expl: starch and glycogen (glucose) |
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starch
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-storage carbs formed by plants
-must be digested to be absorbed |
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glycogen
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-storage carbs of animal tissues
-sorted in skeletal muscle & liver cells -highly branched & large molec. |
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carbohydrate function
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-source of cellular fuel
-dietary carbs convert to glycogen or stored fat |
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lipids
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-insoluble in water
-dissolve readily in other lipids -contain C, H, O -have lower portion of O than carbs -types: triglycerides, phospholipids, steroids |
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triglycerides
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-are neutral fats
-composed of fatty acids and glycerol -fatty acids: linear chains of C, H -glycerol: modified simple sugar -nonpolar molec: don't interact w/ water -efficient & compact form of stored energy -found beneath skin |
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saturated fats
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-one single covalent bonds between carbon atoms
-fatty acid chains are straight & packed closely together to form solid |
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unsaturated fats
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-contain one or more double bonds between carbon atoms
-cause fatty acid chains to kink -more healthy -can't be packed closely to solidify -expl: olive/peanut oils |
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trans fats
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-include margarines & baked products
-oils solidified by addition of H atoms to double carbon atoms -increases heart disease |
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phospholipids
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-modified triglycerides
-phosphorous-containing group and two fatty acid chains tail-nonpolar head-polar |
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steroids
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-flat molec. made of four interlocking hydrocarbon rings
-fat soluble and contain little oxygen -expl: cholesterol |
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eicosanoids
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-diverse lipids derived from a 20-carbon fatty acid
-expl: prostaglandins- roles in blood clotting, inflammation, & labor contractions |
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proteins
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-contain C,H,O,N and many contain sulfur and phosphorus
-expl: enzymes, hemoglobin of blood, and contractile proteins of muscle |
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amino acids
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-are building blocks of proteins
-20 common amino acids -have amine & organic acid group |
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peptide bond
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-bond that links the amino acids
-joined by dehydration synthesis |
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primary structure
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-linear sequence of amino acids composing polypeptide chain
-structure is the backbone of protein molecule |
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secondary structure
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- twists & bends
-common type: alpha (α)-helix (coils) beta (β)-pleated sheet-don't coil, linked side by side by hydrogen bonds to form pleated, ribbonlike structure |
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tertiary structure
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α-helical or β-pleated regions of polypeptide chain fold upon one another to produce compact ball-like, or globular molecule
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quaternary structure
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-two or more polypeptide chains for complex protein
exp: hemoglobin |
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fibrous proteins
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-extended and strandlike
-called structural protein -exhibit only secondary structure, some quaternary -expl: collagen, keratin, elastin -insoluble in water and very stable -provide mechanical support and tensile strength |
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collagen
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-most abundant protein in body
-part of fibrous protein |
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globular proteins
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-compact, spherical proteins
-have tertiary structure, some exhibit quaternary -water soluble, chemically active molecules, and play roles in all biological processes -called functional proteins |
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protein denaturation
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-hydrogen bonds break when pH drops or temp. rises
-causes proteins to unfold & lose specific 3-dimen. shape -can no longer perform roles |
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active sites
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Region on surface of (globular) protein where it binds/interacts chemically with other molec.
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molecular chaperones or chaperonins
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-help proteins to achieve functional three-dimensional structure
-ensures folding is quick & accurate |
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enzymes
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-globular proteins that act as biological catalysts
-chemically specific |
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catalysts
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-substances that regulate & accelerate rate of biochem. rxn
-increase speed of reaction |
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the body utilizes this type of organic molecule first for energy when needed
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carbohydrate
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the type of bond that links amino acids together
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peptide bond
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this compound forms a bilayer in the cell plasma membrane
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phospholipids
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the storage form of glucose in the body
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glycogen
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a classification for fats that contain double bonds and prevent them from freezing
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unsaturated fats
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the concentration of this element in a solution determines the pH
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hydrogen
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the term applied to a protein that has lost its 3-dimensional shape
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denatured
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this type of compound resists abrupt & excessive changes in the pH of a solution
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buffers
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this chemical process uses water to break apart a bond
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hydrolysis
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proteins are classified by shape & configuration. Hemoglobin is classified as a _______type of protein.
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quaternary
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