Lecture 3: Comp Phys Word Scramble
|
Embed Code - If you would like this activity on your web page, copy the script below and paste it into your web page.
Normal Size Small Size show me how
Normal Size Small Size show me how
Question | Answer |
What is a buffer? | conjugate acid-base pair that prevents or minimizes changes in pH with the addition of small amounts of acid or base substances |
Define pH? | physical property of a solution determined by conjugate acid/base pair at equilibrium |
The depletion of H+ ________ pH. | increases |
What happens when you add an acid to a system? | the base reacts with the H+ and the equilibrium shifts to acid |
What happens when you add a base to a system? | the acid reacts with the OH- and the equilibrium shifts to base |
What is the equation to calculate pH? | pH=pKa+log [conjugate base]/[conjugate acid] |
Why are buffers important? | they are important for maintaining homeostasis |
What is the pH of human plasma? | 7.35-7.45 |
How is human plasma pH maintained? | by weak salts, acids as conjugate pairs, bicarbonate system, phosphate buffering system |
What is acidosis? | pH below 7.35 |
What is alkalosis? | pH above 7.45 |
What is an enzyme made of? | proteins which are made of amino acids with ionizable groups |
What is a zwitterion? | ionic form of amino acids at pH 7 |
When are ionic groups of proteins lost? | when peptide bonds are formed |
What makes an amino acid basic or acidic? | containing an additional ionizable group |
What is crutial to enzyme function? | the ionizable groups becuase they allow the protein chains to be linked or confromed in a particular shape |
Define: enzyme | biocatalytic protein; most efficient catalysts known |
What are 3 unique features of enzymes? | Efficiency, specificity, and regulation |
define: efficiency (in terms of enzymes) | enzymes can catalyze a reaction almost immediately |
What is an example of enzyme efficiency? | enzyme cholinesterase: breaks down acetyle choline almost immediately for muscle contractions |
What is specificity? (in terms of enzymes)? | most enzymes exhibit relative specificity i.e. catalyze the same type of reaction with realitively similar structured substances |
What is an example of enzyme specificity? | enzyme monoaminoxidase: catalyzes norepinphrine, serotonin, dopamine |
What type of regulation do most enzymes use? | allosteric regulation |
What is allosteric regulation? | enzymes bind on some region of the enzyme to alter active site so S is not recognized or enhavces the function |
What are the two types of specificity? | Relative specificity and absolute specificity |
What is relative specificity? | enzymes catalyze the same types of reactions with similar structured substances |
What is absolute specificity? | enzymes catalyze only one type of reaction with a specific substrate |
What is an example of an enzyme that uses absolute specificity? | glycerol kinase |
Define: active site (in terms of enzymes) | region of an enzyme that recognizes a given substrate and catalyzes the conversion of a substrate to a product |
What happens to an enzyme during catalysis reactions? | the reaction will start and end with the enzyme i.e. neither created nor destroyed |
What are the 3 types of reactions at the active site? | bond-strain catalysis, acid-base catalysis, and orientation catalysis |
What is bond strain catalysis? | S binds to enzyme which causes bond strain and increases the probability that the bond will break |
What is acid-base catalysis? | active site has an ionizable r-group and they interact as proton donors or acceptors |
what is orientation catalysis? | substrate is held in an orientation that optimizes/maximizes the probability of a reaction |
What role does temperature play in reaction rates? | higher temperatures may increase reaction rates |
What happens to enzymatic reaction rates at low temperatues? | at low temperatures the enzyme is cold inactiavated |
In cold inactivated enzymes, the inactivation is ______. | reversible |
What happens to intermediate to high temperatures on enzymatic reactions? | as the temperature increases, the conversion from S-P increases due to increase in kinetic activity |
What hapens to enzymatic reaction rates at extremely high temperatures? | enzyme activity completely stops because the enzyme is denatured |
In high temperature inactivated enzymes, the inacivation is _______. | irriversible |
What role does pH play in enzymatic reactions? | most reactions have an optimum pH at which the reaction rate is at it's most efficient |
What does altering pH from optimum do? | effects the ionizable groups of amino acids that will make up the enzyme i.e. affect confirmation and alter recognition of the substrate |
What do many enzymes depend on for optimum activity or presence of activity? | cofactors |
What are cofactors? | non-protein substance |
What is an enzyme in the absens of a cofactor/ with low or no activity? | apoenzyme |
What is an enzyme in the presence of a cofactor? | haloenzyme |
What are the two categories of cofactors? | inorganic and organic |
What are inorganic cofactors? | usually ions, Zn2+,Mg2+,Fe2+, Ca2+ |
What are organic cofactors? | often derived from vitamins, NAD+ |
What are organic cofactors often called? | coenzymes |
Define: vitamins | essential nutrients not derived endogenously |
What are fat soluble vitamins? | A,E,D |
What are water soluble vitamins? | B series |
How many role sdo cofactors have? | 2 |
What is the first role of cofactors? | alter substrate or enzyme conformation to maximize interaction |
What is the second role of cofactors? | participate in reaction as a second substrate by doating or accepting a particular chemical grouping |
Enzymes can be ______ by both physiological and pharmacological agents | inhibited |
What are the two types of pharmacological enzyme inhibitors? | irreversible inhibitors and reversible inhibitors |
What are irriversible inhibitors? | inhibitors that bind to the active site and are not released |
What is an example of an irriveresible inhibitor? | organophosphate nerve gas |
How do orgnaophosphate nerve gases work? | blocks the reaction |
What are reversible inhibitors? | inhibitors that may be removed |
What are the two types of reversible inhibitors? | competitive inhibitors and noncompetitive inhibitors |
What are competitive inhibitors? | reversible inhibitors that bind to the active site, but can be displaced in the presence of high substrate concentrations |
What are noncompetitive inhibitors? | reversible inhibitors that bind the enzyme outside of the active site and cause an allosteric or conformational change that alters active sites |
How are noncompetitive inhibitors reversed? | they are reversed as the inhibitor is released and degrated |
Created by:
kenzigustafson
Popular Biology sets