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Anatomy Biochemistry

Human Anatomy (Marieb)

Salt ionic compound containing cations other than H+ and anions other than OH- (dissociate in water)
Electrolyte substance that conducts an electrical current in a solution (all ions are electrolytes) (dissociate in water)
What is one of the most important functions of the kidney? Maintain correct ionic balance in body fluids required for homeostasis
List the 5 properties that make water vital to life High heat capacity, high heat of vaporization, Polar solvent properties, reactivity, cushioning
Acid a substance that releases Hydrogen ions (H+) in detectable amounts (also called proton donors) Electrolytes
Bases A substance that takes up Hydrogen ions (H+). also called proton acceptors. Electrolytes
Bicarbonate ion (HCO3-) an importance base found in blood
pH units measures the relative concentration of hydrogen ions in various fluids
What happens when acids and bases mix? they react to form water and a salt
neutralization reaction reaction when an acid and base mix. They neutralize and form water anda salt
Buffers Chemical systems that resist abrupt and large swings in pH levels
Why is Carbon so important Unlike any other small atom, it is electroneutral
Polymers chainlike molecules made of many smaller, identical or similar units (monomers) joined together
Monosaccharides Simple sugars or single-chain structures containing from 3 to 7 carbon atoms
Disaccharide double sugar, or two monosaccharides joined by dehydration synthesis
Polysaccharides polymers of simple sugars. Large and fairly insoluble they are ideal storage products.
Glycogen Polysaccharide (storage carbohydrate) of animals
Lipids insoluble in water, but soluble in other lipids or organic solvents
Triglycerides also called neutral fats. called fats when solid and oils when liquid. very large molecules. composed of fatty acids and glycerol
Saturated fats single covalent bonds between carbon atoms form single chains resulting in solid fats. Animal Fats (Solid at room temp)
unsaturated fats contain one or more double bond between carbon atoms resulting in liquid oils Plant oils (liquid at room temp)
Trans fats Oils that have been solidified by the addition of hydrogen atoms at the point of the double bonds
Phospholipids modified triglycerides (contain 2 instead of 3 fatty acid chains)
Steriods fat soluble, containing little oxygen. 4 interlocking hydrocarbon rings
Amino acids building block of proteins. can act as either an acid or a base
Peptide bond bond joining the amine group of one amino acid to the acid carboxly group of a second amino acid with the loss of water
Macrololecules large, complex molecules containing over 100 to 10,000 amino acids
alpha-helix structure of protein coiled structure - like a slinky toy always link different parts of the same chain together
beta-sheet structure of protein pleated, ribbon like structure - like an accordion bellow may link different chains or different parts of the same chain
fibrous proteins also called structural proteins - extended and strand like insoluble in water and very stable Structural proteins
what is the most abundant protein in the body collagen
globular proteins also called functional proteins - compact, spherical water soluble and chemically active Transport proteins Hydrogen bonds Can be disrupted by pH imbalance Depends on active sites
denatured condition when a protein unfolds and loses its 3-dimensional shape due to temperature or pH changes
Enzyme globular protein that acts as a biological catalyst Binds to substrate Denaturation disrupts process
Activation Energy The amount of energy required to push a reactant to the level necessary for action
Nucleic acids the largest molecules in the body composed of carbon, oxygen, hydrogen, nitrogen, and phosphorus
What are the two major classes of Nucleic acids Deoxyribonucleic acid (DNA) and Ribonucleic acid (RNA)
Nucleotides structural units of nucleic acids
What are the 5 major varieties of nitrogen containing bases that contribute to nucleotide structure adenine (A), guanine (G), cytosine (C), thymine (T), and uracil (U)
Double helix spiral staircase like structure of DNA
What are the complementary bases A always bonds to T G always bonds to C
DNA Long, double-stranded polymer consisting of A, G, C and T main sugar is deoxyribose Gives instruction to RNA Replicates cell division
RNA carries out the orders for protein synthesis issued by DNA. Single strands of nucleotides consisting of A, G, C, and U Main sugar is Ribose
Adenosine triphosphate (ATP) Organic molecule that stores and releases chemical energy (glucose) for use in the body Energy can be used immediately Directly powers chemical reactions in cells
What are the 2 classes of compounds Organic inorganic
Inorganic compounds don't contain carbon (except CO2 and CO) water, salts, and many acids and bases
organic compounds contain carbon, usually large, and covalently bonded carbohydrates, fats, proteins and nucleic acids
What is the normal pH level for blood between 7.35 and 7.45
What are the 4 main kinds of organic compounds Carbohydrates Lipids Proteins Nucleic Acids
What are the 3 classes of carbohydrates Monosaccharides (One sugar), Disaccharides (Two sugars), Polysaccharides (many sugars)
What are the two major functions of carbohydrates Source of Cellular fuel (glucose) Structural molecules
What two kinds of foods are carbohydrates sugars starches
What are the 3 main functions of Lipids Energy storage Insulation Protection
What kind of organic compound are steroids Lipids
What kinds of organic compound are triglycerides? Lipids
What makes phospholipids unique they have a head an tail region that are each polarized
What is the most important steroid Cholesterol
List 4 common steroids found in the body Cholesterol Vitamin D Steroid hormones Bile Salts
Are proteins polymers or monomers Polymers
What are the monomers found in proteins amino acids
What elements are common to proteins Carbon Hydrogen Oxygen Nitrogen sometimes Sulfur and Phosphorus
What kind of bond joins amino acids covalent bonds called peptide bonds
Amino acids contain what two groups amine group (acts like base) acid group (acts like acid)
All amino acids have the same structure except for which part the R group
What are amino acids with less than 50 chains called Polypeptide
What accounts for the different function in amino acids their chain sequence variation
What are the four levels of protein structure in amino acids 1. primary - chain of amino acids 2. secondary - formation of helices or sheets 3. teritary - helices or sheets fold up to form globular molecules 4. quaternary - two or more polypeptide chains, each with its own first three levels combine
Name 2 examples of fibrous proteins Collagen Keratin
Give 3 examples of Globular proteins Antibodies Hormones Enzymes
What are the three kinds of RNA Messenger RNA (mRNA) Transfer RNA (tRNA) Ribosomal RNA (rRNA)
What is the structure of RNA Adenine containing RNA nucleotide with two additional phosphate groups
What are three functions of ATP Transport work - activates proteins to transport solutes across cell membranes Mechanical work - contract proteins in muscle cells so they can shorten Chemical work - provides energy for chemical reactions
What is the pH range for acidic cubstances 0 to 6.999 (below 7)
What is the pH range for alkaline subtances 7.0001 to 14 (above 7)
Created by: twolden1