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Ch. 3-5, 8

Biochemistry

QuestionAnswer
What is the weakest type of bond? hydrogen bonds
What are hydrophilic interactions? interactions with H2O
What is the strongest type of bond? covalent bonds
What is the chemistry of water? polar covalent bonds; H2O molecules form H-bonds with each other
Why are we studying water All life occurs in water; inside and outside of cell
What is cohesion & adhesion surface tension & capillary action cohesion: the bonding of water molecules that pull each other along adhesion: the attraction of water molecules to other substances
What does it mean that water is the greatest solvent of life? many molecules dissolve in H2O, hydrogen bonds can break up substances
What property describes why ice floats lower density as a solid
What is moderation of a temperature high specific heat = water stores heat high heat of vaporization = heats & cools slowly
How does water get to the top of trees? transpiration is built of cohesion and adhesion; water goes through cell walls and permeable membranes
What makes water a good solvent polarity
What is hydrophilic substances that have an attraction to water; mainly polar.
What is hydrophobic substances that do not dissolve in water, usually non-polar
What is polar unevenly charged
Why is it important that ice floats? so that bodies of water don't freeze solid, allows ice to survive in water.
How does freezing affect the layers of the ocean water freezes on top so if ice sank than the water would freeze bottom up and kill life inside water
How is ice formed? Hydrogen bonds form a crystal lattice
What is specific heat? H2O is resistant to change in temperature
What does it mean that water moderates temperature water stores heat and releases it.
more hydrogen ions? acidic
less hydrogen ions basic
[H+] and [-Oh] is equal neutral
what is the pH of a solution that is 10^(-7) seven
what do buffers do in our bodies keep our body at a certain pH
Why is it important that our body maintains a certain pH we would die if it didn't
What are some ways that buffers maintain that body's pH? donates [H+] when falls, absorbs when too high.
What are the six most abundant elements of life (CHNOPS) carbon, hydrogen, nitrogen, oxygen, phosphate, sulfur
What do we study carbon all life is built on carbon
What is organic chemistry the study of carbon compounds
What are the properties of carbon? bonding properties, 4 stable covalent bonds, basis of all life, different forms in which it exists
What are hydrocarbons? combination of carbon and hydrogen
What are properties of hydrocarbons non-polar, stable, very little attraction between molecules, gas at room temperature
What are macromolecules smaller organic molecules join together to form large molcules
What are the four major classes of macromolecules lipids, proteins, nucleic acids and carbohydrates
What are polymers and what are their building blocks? long molecules built by linking repeating blocks in a change; monomers are building blocks
Which type of bonds hold together monomers covalent bonds
What is the name of the process that binds together monomers dehydration synthesis
What is the name of the process that breaks about monomers hydrolysis
Which process loses a water molecule dehydration synthesis
which process adds a water molecules hydrolysis
What does hydrolysis require energy and enzymes
What is an example of hydrolysis digestion
What is an example of dehydration synthesis condensation reaction
What does dehydration reaction require energy and enzymes
What are the building blocks of carbohydrates monosaccharides
What are that functions of carbs energy, raw materials, energy storage, structural compounds
Most of the names of sugars end in what? -ose
How are sugars classifies by the number of carbons
When is the energy stored in carbon bonds harvested? in cellular respiration
example of monosaccharide glucose
example of disaccharide sucrose
polysaccharides starch
are polysaccharides reversible yes; easily
How do certain polysaccharides polysaccharides differ? molecular structure, isomers,
what is a structural isomer same elements, different structure
What is cellulose most abundant organic compound on earth, cell walls and such
What are ruminants? able to digest cellulose through four chamber stomach and chew on cud
Hind-gut fermenters eat waste
What is the most structurally &functionally diverse group proteins
What are the monomers of proteins amino acids
What make up amino acids central carbons, amino groups, carboxyl gropus, r groups
What are r groups variable groups that are different for each amino acids (side chain)
How is sulfur important it forms disulfide bridges, (covalent crosslinks between sulfhydryls/stabilizes 3D structure)
What are peptide bonds? covalent bonds between two amino acids/ carbon-nitrogen bond
What does it meant that polypeptide chains have direction? can only grow in one direction
What does function depend on? structure
primary structure amino acid sequence-peptide bonds determined by DNA
secondary structure k groups H bonds
What is tertiary structure r groups hydrophobic interactions and disulfide bridges
quaternary structure multiple polypeptide chains, hydrophobic interactions
What is protein denaturation unfolding a protein,
What are some causes of protein dneaturation extreme conditions of temperature pH and salinity
what does protein denaturation destroy functionality
function of nucleic acids genetic materials, stores info, genes, blueprint for making proteins
What are the two main nucleic acids DNA & RNA
difference between deoxyribose and ribose deoxyribose lacks an oxygen atom on the second carbon in the ring
What is the monomer of nucleic acids nucleotides
What makes up a nucleotide pentose sugar, nitrogen base and phosphate group
What elements are in lipids carbon, hydrogen and oxygen
What are the "family groups" of lipids fats phopholipids and steroids
lipids do not form polymers
What makes up fats glycerol + fatty acid (long hydrocarbon chain)
what do fats store energy
what are other functions of fats cushion organs, insulate body
What are saturated fats no double carbon bonds, straight, solid at room tempurature
What are unsaturated fats double bonds, kinks, liquid at room temperature
What are pohpholipids glycerol and 2 fatty acids
How are phospholipids assembled when they are by water hydrophilic heads attracted to H2O and hydrophilic tails "hide" from H2O
What is the structure of steroids? 4 fused C rings
How are different steroids crated? by attaching different functional groups to rings
How is cholesterol important important cell component: animal cell membranes, precursor of all other steroids
What are some important sex hormones? estradiol, and testosterone
How much energy transfers from one trophic level to the next? 10%
Life is built on what? chemical reactions; transforming energy from one form to another
What is metabolism chemical reactions of life
What some examples of metabolic pathways dehydrations synthesis and hydrolysis
catabolic reactions braking down
anabolic reactions building
exeronic reactions release energy/ catabolic
endergonic reactions require input of energy/ anabolic
What is coupling exergonic reactions with endergonic reactions give required energy to organisms
Why don't downhill reactions happen spontaneously because covalent bonds are stable bonds
What is activation energy energy required for the reaction
What helps reduce activation energy catalysts
Why are catalysts important activation energy required would kill us without them
What are enzymes biological catalysts required for most biological reactions
What is a substrate reactant that binds to enzyme
what is a product end result
What is the active site where te subtrate goes
What tare the properties of enzymes reactions specific (each enzyme works with a specific substrate), not consumed in reaction, affected by cellular conditions
What is induced fit substrate binding causes enzyme to change shape leading to a tighter fit; conformation fit
What factors affect enzyme function enzyme concentration, substrate concentration, temperature, pH, salinity, activators, and inhibitors
What does it mean that the reaction rate levels off (enzyme concentration) substrate becomes limiliting factor, not all enzyme molecules can find substrate
What does it mean that the reaction rate levels off (substrate concentration) all enzymes have active site engage; enzyme is saturated; maximum rate of reaction
What is optimum different enzymes function in different organisms in different environments
What are cofactors non-protein small inorganic compounds that bind within enzyme molcule
what are coenzymes non-protein organic molecules, bind temporarily or permanently to enzyme near active site
What compounds regulat enzymes competitive inhibitor, noncompetitive inhibitor, reversible inhibitor, feedbakck inhibition
What is a competitive inhibitor inhibitor and substrate compete for active site
how is a competitive inhibitor overcome increasing concentration
noncompeitive inhibitor inhibitor binds to site other than active site; causes enzyme to change shape
irreversible inhibition competitor permantently binds to active site;
What is allosteric regulation conformational changes by regulatory molecules;
inhibitors keeps enzyme in inactive form
activators keeps enzyme in active form
what are metabolic pathways cahin of reactions
what do metabolic pathways link endergonic and exergonic reactions
what is feedback inhibition regulation and coordination of production
What is cooperativity substrate acts as an activator; substrate causes conformational change in enzyme; favors binding of substrate at 2nd sit; makes enzyme more active and effective.
Created by: 3j0mk1