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54 terms

A&P: The Chemistry of Life

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element
the simplest form of matter to have unique chemical properties
how many elements play a biological roll?
24
What 6 elements make up most of the body weight and what is the %?
oxygen, carbon, hydrogen, nitrogen, phosphorous, and calcium. makes up 98.5% of body weight
minerals
inorganic elements that are extracted from soil by plants (3/4 in body is Ca and P)
electrolytes
needed for nerve and muscle function are mineral salts
isotopes
varieties of the same element that differ only by atomic mass (different number of neutrons)
Atomic weight
accounts for the fact that an element is a mixture of isotopes
Radioisotopes
unstable isotopes that breakdown or decay to a more stable isotope by releasing radiation, some harmless but some harmful to tissues
ionizing radiation
deadly in high doses, mutagenic and carcinogenic in small doses
physical half life
the time it takes 50% to decay into a more stable state
Electrolytes
salts that ionize in water and are capable of conducting an electric current
electrolyte importance
chemical reactivity, osmotic effects (influence water movement), electrical effects on nerve and muscle tissue
free radicals
chemical particles with an odd number of electrons, antioxidants neutralize them
Van Der Waals Forces
weak, attraction between neutral atoms
Adhesion
tendency of one substance to cling to another
cohesion
tendency of like molecules to cling to one another
decomposition reaction
AB-> A+B
synthesis reaction
A+B-> AB
exchange reactions
AB + CD-> AC + BD
reversible reactions
can go in either direction under different circumstances
metabolism
all the chemical reactions in the body
catabolism
energy releasing (exergonic) decomposition reactions, breaks covalent bonds, produces smaller molecules
anabolism
energy storing (endergonic) synthesis reactions, requires energy input, driven the energy released by catabolism
oxidation
any chemical reaction which a molecule gives up electrons and releases energy, molecule oxidized in this process, electron acceptor in this process is oxidizing agent
reduction
any chemical reaction in which a molecule gains electrons and energy, molecule is reduced when it accepts electrons, molecule donating electron is reduction agent
oxidation- reduction reaction
oxidation of one molecule is always accompanied by reduction of another
organic chemistry
the study of compounds containing carbon
biochemistry
the study of molecules that compose living things
what are the 4 categories of bio- compounds
carbogydrates, lipids, proteins, nucleotides and nucleic acids
functional groups
small clusters of atoms attached to carbon back bones
what are the 5 functional groups in ppt?
hydroxyl, methyl, carboxyl, amino, phosphate
hydroxyl
(-OH) occurs in sugars, alcohols
methyl
(-CH3) occurs in fats, oils steroids, amino acids
carboxyl
(-COOH) occursin amino acids, sugars, proteins
amino
(-NH2) occurs in amino acids and proteins
phosphte
(-H2PO4) occurs in nucleic acids and ATP
polymerization
joining monomers to make a polymer
dehydration synthesis
how living cells form polymers, a hydroxyl (-OH) group is removed from one monomer, and a hydrogen (H+) from another
hydrolysis
a water molecule ionizes into -OH and H+, covalent bond linking one monomer to the other one is broken, the -OH is added to one monomer and the H+ is added to the other
carbohydrates
hydrophilic, general formula (CH2O)n, made up of monosaccharides
polysaccharides
glycogen (energy storage in animals), starch (energy storage in plants, cellulose
Carbohydrate functions
quickly mobilized source of energy, all digested carbs are converted to glucose,
protein
a polymer of amino acids
amino acid
central carbon with 3 attachments, amino group (NH2), carboxyl group (COOH), and radical group (R) group. (properties are determined by the R group)
peptide
any molecule composed of two or more amino acids joined by peptide bonds
peptide bond
joins the amino group of one amino acid to the carboxyl group of the next
primary structure
protein's sequence amino acids which is encoded in the genes
secondary structure
coiled or folded shape held together by hydrogen bonds (alpha helicies or beta pleated sheets)
tertiary structure
further bending and folding of proteins into globular and fibrous shapes
glubular proteins
compact tertiary structures well suited for proteind embedded in cell membranes and proteins that must move freely in body fluid
fibrous proteins
slender filaments better suited for roles as in muscle contraction and strengthening the skin
quaternary structure
associations of two or more polypeptide chains
protein functions
structure, communication, membrane transport, catalysis, recognition and protection, movement, cell adhesion
nucleotides
has 3 components: nitrogenous base, sugar, one or more phosphate group ex) ATP