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Honors Bio - Bio Chem Test


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what is biochemistry
the study of biologicall active, organic (contains carbon) compounds
5 reasons why carbon is so important
*forms 4 covalent bonds
*bonds to many different elements
*single and double bonds
*carbon allows for an infinite variety of structures, therefore infinite variety of functions
*forms rings, chains, branching chains
slogan for chapter
DEFINE Carbohydrate
an organic compound present in the cells of all living thins and a major organic nutrient for humans
ELEMENTS in Carbohydrates
C, H, O
MONOMERS Carbohydrates
H:O Ratio in Carbohydrates
General Formula for Carbohydrates
CH20 "Carbon Water"
function of monosaccharides in carbohydrates
*used to build complex carbs
*quick access to energy
what are 2 monosaccharides bonded together
what are 3+ monosaccharides bonded together
DEFINE polymerization
the proccess of linking monomers to form polymers
Polymerization is what type of reaction?
dehydration synthesis
revearse polymerization
FUNCTION dissacharides
*transports sugars in plants
FUNCTION polysaccharides
*short term energy storage- stored in glycogen
*structural support
DEFINE lipid
a kind of organic compoundthat is insoluble in water, such as fats and steriods
C, H, O
ratio between H and O in lipids
which stores more energy, lipids or carbohydrates?
lipids = 2x the energy storage as carbohydrates
List 9 Functions of lipids
*long term energy storage
*protection, cushioning
*cell membrane
*chemical messengers
*creates wax
*makes up saturated and unsaturated fats
*makes up hormones
MONOMERS in lipids
fatty acids, glycerol
2 saturated fats
*animal fats
2 unsaturated fats
*plant oils
*fish oils
why are sat. fats worse for you?
straight lines, so can solidfy more easily, causes arties and clots
structure of a unsat. fat
curly, becuase of carbons double bond with eachother
fatty acid structure
H H H H =O
WHAT IS A CARBOXyL GROUP/carboxyl acid
what parts of the fatty acid are polar/nonpolar
the=O and the OH are polar, the rest are not
ELEMENTS proteins
what is the structure of a protein like?
MONOMERS in proteins
amino acids
how many amino acids and how do they connnect to chains
20 types, and in any order
what determines function?
structural diversity
name 7 functions of proteins
*transport: pumps, channels across membranes
*transports: long distance
4 levels of a protein structure
1) primiary (polypeptide chain)
2) secondary structure
3)tertiary structure
4) quatonary structure
check answer in the texty
what does a polypeptide chain (primary level in protein) determine?
determines how the protein will fold, therfore defining its structure
DEFINE polypeptide chain
lineas chain of amino acids linked by peptide bonds
what are the two shapes of the secondary structure in a protien
spiral or swiggles then a big bowly thing
what bonds with what to create the secondary structure
H bonds with amino and carboxyl
how is the tertiary structure in a protien held together
by interactions between R groups, ionic bods, H bonds, covalent disulfide bonds
when do most proteins become functional
at the tertiary structure
DEFINE adhesion
the attractive force between unlike substances
DEFINE capillarity
the reaction of a liquid surface with a solid, a capillarity allows water to creep up the interior of a narrow vessel
DEFINE cohesion
the attraction of like molecules to eachother
DEFINE hydrogen bond
a weak chemical bond between the hydrogen atom in one molecule and a negativley-charged region of another molecule
DEFINE polar
a compound with one side hacing a negative charge and the other side having a positive charge
DEFINE adenosine triphosphate
(ATP) a molecule present in all living cells and acting as an energy source for metabloic processes
DEFINE functional group
a structural building block that determines the characteristics of a chemical compound
DEFINE condensation reaction
a chemical reaction, also called dehydration synethesis, in which one molecule isproduced (H2O)
DEFINE hydrolysis
the splitting of a molecule through reaction with water
DEFINE macromolecule
a very large oraganic molecule composed of many smaller molecules
DEFINE monomer
a repeated, single-molecule unit in a polymer
DEFINE polymer
a compound consisting of repeated linked monomers
DEFINE amino acid
a carboxylic acid with an amino group; one of the 20 monomers that form a protein
DEFINE dipeptide
a formation from two amino acids bonded together by means of condensation reaction
DEFINE disaccharide
a double sugar formed from two monosaccharides
DEFINE fatty acid
a monomer that is part of most lipids
DEFINE hydrophilic
reffering to the molecular attraction to water
DEFINE hydrophobic
reffering to the molecular repulsion of water
DEFINE isomer
one of the two or more compounds that differ in structure but not in molecular composition
DEFINE monosaccharide
a simple sugar suc as frutose or glucose
DEFINE nucleic acid
an organic molecule, DNA or RNA, that stores and carries important information for cell function
DEFINE nucleotide
a monomer of dna and RNA consisting of a nitrogen base, a sugar, and a phosphate group
DEFINE peptide bond
a covalent bond between two amino acids
DEFINE phospholipid
a complex lipid having two fatty acids joined by a molecule of glycerol
DEFINE polypeptide
a long chain of several amino acids
DEFINE polysaccharide
a complex carbohydrate composed of three or more monosaccharides
DEFINE protein
an organic compound composed of one or two more chains of polypeptides which in turn are formed from amino acids
DEFINE ribonucleic acid (RNA)
a nucleic acid composed of a single strand and distinguished from DNA by containing ribosome and uracil
DEFINE steriod
a lipid in which the moleculeis composed of four carbon rings
DEFINE substrate
a part, substance, or elment that lies beneath and supports and supports another; the reactant in any enzyme-catalyzed reaction
DEFINE triglyceride
a lipid made up of three fatty acid molecules and one glycerol molecules
difference between condensation reaction hydrolisis
condensation reaction links monomers, but hydrolisis does just the oppisite
lock-and-key method
when an enzyme can only atach too a certain shape, enzyme flexes to conform to reactants shape, then enzyme is unchanged and is reused by another reactant

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