Help
Options
Didn't know it?
click below
click below
Knew it?
click below
click below
Don't Know
Remaining cards (0)
Know
retry
shuffle
restart
0:00
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
BIO Exam 2
Intro to Biology 1801 Exam 2 flashcards/study set
| Question | Answer |
|---|---|
| Cells produce thousands of distinct ___. | proteins |
| What are the building blocks of proteins? | Amino Acids |
| How many amino acids are most proteins made of? | 20 amino acids |
| What are the properties of amino acids determined by? | R-group |
| What is another name for an "R-group"? | Side chains |
| What are the 3 groups that side chains are grouped into? | Charged, uncharged polar, uncharged nonpolar |
| In charged side chains, does it include acidic, basic, or both elements? | both |
| What 2 features affect the R-group (or side chains) solubility? | Polarity and Charge |
| Charged and polar are ____. | Hydrophilic |
| Nonpolar side chains are ___. | Hydrophobic |
| True or false (Correct statement if false): Hydrophilic side chains interact readily with water. | True |
| True or False (Correct statement if false): Hydrophobic side chains DO NOT interact with water. | True |
| Proteins are considered ___. | Macromolecules |
| Large molecules are made of smaller ___. | Subunits |
| What are subunits called? | Monomers |
| What is the process called when monomers link together? | Polymerize |
| When monomers link together, what do they form? | Polymers |
| __ __ are the monomers that make up proteins. | Amino Acids |
| What is the process that monomers polymerize through? | Condensation reactions |
| What is another word for the process of condensation reactions? | Dehydration synthesis |
| Through dehydration synthesis, the proteins lose a ___ molecule. | water |
| What is the reverse reaction of condensation reaction? | Hydrolysis |
| What process breaks down polymers by adding a water molecule? | Hydrolysis |
| Name the process: Monomer in, water out. | Condensation reaction |
| Name the process: Water in, monomer out. | Hydrolysis |
| Amino Acids polymerize when a bond forms between a ___ group and one ___ ___ and an amino group to another. | carboxyl; amino acid |
| What is the resulting C-N bond called that forms through amino acid polymerization? | Peptide bond |
| What causes a peptide bond to have characteristics of double bonds? | When a pair of valance electrons on nitrogen & oxygen are partially sharing the C-N bond. |
| Peptide bonds are considered the ___. | backbone |
| What is a chain of many amino acids called? | Polypeptide |
| ____ are the complete, function form of molecules. | Proteins |
| Proteins haven unparalleled diversity of ___. ___, and ___ properties. | size, shape, chemical |
| Proteins serve ___ function in cells. | diverse |
| Why do proteins serve diverse functions in cells? | Because structure gives rise to function. |
| Collagen has ___ strands. | Triple |
| True or false (correct statement if false): Proteins are the most diverse class of molecules known. | True |
| What is proteins primary structure? | Its unique sequence of amino acids |
| The number of primary structure is practically ___. | Limitless |
| __types of amino acids are available. | 20 |
| What is the length range for protein structure? | Two amino acids to tens of thousands |
| Primary structure is fundamental to the ___ levels of protein structure. | higher |
| A ___ amino acid can radically change and alter a proteins function. | single |
| Is this a normal sequence of residues or single change sequence: Pro (5) --> Glu (6) --> Glu (7) | Normal |
| Changes in primary structure affect ___ function. | Protein |
| What structure is formed by hydrogen bonds between certain amino acids (carbonyl group-amino group)? | Protein secondary structure |
| α-helices and β- pleated sheets are example of what kind of structure? | Proteins secondary structure |
| A ___ structure of a polypeptide results from interactions between R-groups or between R-groups and the peptide backbone. | Tertiary |
| A tertiary structure has interactions between ___ groups. | R-groups |
| A tertiary structure of a polypeptide is a result from R-groups and the ___ backbone. | peptide |
| What 2 movements contribute to the distinctive dimensional shape of a polypeptide. | Bending and folding |
| What are the five important types of R-group interactions? | Hydrogen bonds, hydrophobic interactions, Van der Waals interactions, covalent disulfide bonds, and ionic bonds. |
| A Van der Waals interactions is a weak electrical interaction between ____ side chains. | hydrophobic |
| Covalent disulfide bonds form bridges between two _____ groups. | sulfhydryl |
| The bonding of two or more distinct polypeptide subunits produces ____ structure. | quaternary |
| Some cells contain ___ machines. | molecular |
| What are molecular machines? | groups of multiple proteins that carry out a particular function |
| Proteins with quaternary structure have multiple ____. | polypeptides |
| What is the correct level of protein structure? | Primary, Secondary, Tertiary, Quaternary |
| The sequence of amino acids in a polypeptide is the description of what level in the protein structure? | Primary |
| The formation of a-helices and B-pleated sheets in a polypeptide is what level in the protein structure? | Secondary |
| Overall three- dimensional shape of a polypeptide that contributes to secondary structures is what level of protein structure? | Tertiary |
| On the ___ level, the shape produced by combinations of polypeptides is the description. | quaternary |
| The Primary level is stabilized by ___ bonds. | peptide |
| The Secondary level is stabilized by hydrogen bonding between groups along the ___ - ____ backbone. | peptide-bonded |
| ____ folding is often spontaneous. | Protein |
| ____ ___ help protein fold correctly in cells. | Molecular chaperones |
| A ___ (unfolded) protein is unable to function normally. | denatured |
| True or False (if false correct the statement): Some proteins are regulated by controlling where or when they are folded into inactive shapes. | false; active |
| ___ can be infectious to the protein shape. | misfolding |
| ____ are improperly folded forms of normal proteins. | Prions |
| Prions can induce normal protein molecules to change their __ to the altered form. | shape |
| Prion infectivity is linked to __. | structure |
| What is the most important protein function? | Enzymes |
| What is a protein that functions as a catalyst? | An enzyme |
| What is the name of the location on an enzyme where substrates bind and react? | the active site |
| __ and __ fit together like a lock and key. | substrate and enzyme |
| Photosythesis produces __ and __. | O2 and glucose |
| Cellular respiration produces ___ and ___. | CO2 and H2O |
| Where does photosynthesis gain its energy to start the process? | sunlight |
| ___ energy is energy of motion. | Kinetic |
| __ energy is energy of molecules moving. | thermal |
| __ energy is energy that is stored in position of configuration. | Potential |
| __ energy is energy stored in chemical bonds. | chemical |
| Under the 1st law of Thermodynamics, energy cannot be __ nor __. | created nor destroyed |
| Under the 1st law of Thermodynamics, energy can only be ___ and ___. | transferred and transformed |
| With Energy in a water fall, what kind of energy is known to be at the top of the cliff, right before it falls? | Potential energy |
| With energy in a water fall, what kind of energy is known to be as it is falling down the cliff (mid fall)? | Kinetic Energy |
| Energy travels from areas of ___ concentration to areas of ___ concentration. | high to low |
| What two factors does the potential energy of a molecule depend on? | configuration and position |
| As a bond goes from nonpolar --> polar, the potential energy is decreasing or increasing? | decreasing |
| Equal electron sharing has a __ charge. | nonpolar |
| Unequal electron sharing has a __ charge. | polar |
| A C--H bond is the ____ and weakest bond. | longest |
| A O--H bond is the shortest and ____ bond. | strongest |
| Potential energy ___ as the length of the bonds decrease and the ___ of the bonds increase. | length; strength |
| If the products have shorter, stronger covalent bonds, than the reactions potential energy in the bonds ___. | Decrease |
| The 2nd law of Thermodynamic states that total ___ always increase in a system. | entropy |
| Gibbs Free Energy (G) determine whether a reaction is_____ or requires added ___ to proceed. | spontaneous; energy |
| The ___ free-energy change equation is ΔG = ΔH – TΔS. | standard |
| ΔH in the standard free-energy change equation stands for what? | change in enthalpy |
| ΔS is the standard free-energy change equation stands for what? | change in entropy |
| T in the standard free-energy change equation stands for what? | temperature |
| ΔG < 0 is a ___ reaction. | spontaneous |
| ΔG < 0 is considered to be ___. | exergonic |
| ΔG > 0 is a _____ reaction that requires energy input to occur. | nonspontaneous |
| ΔG > 0 is considered to be ___. | endergonic |
| ____ reactions may be drive using chemical energy. | nonspontaneous |
| ____: the loss of an electron(s) | oxidation |
| ___: gain of an electron(s) | Reduction |
| Oxidation reactions are considered to be ___ reactions. (releasing energy) | Exergonic |
| Reduction reactions are considered to be __ reactions. (requires energy) | Endergonic |
| Endergonic reactions ___ energy. | require |
| Exergonic reactions ____ energy. | release |
| Electrons can be ___ completely from one atom to another. | transferred |
| Electrons can shift their position in ___ bonds. | covalent |
| Electrons are usually accompanied by a ___ (H+). | Proton |
| Reduction often ____ hydrogens (Hs). | adds |
| Oxidation often _____ hydrogens (Hs). | removes |
| Electrons can be transferred from an electron ___ to an electron ___. | donor; acceptor |
| Acceptor generally ___ potential energy. (gains/loses) | gains |
| Flavin adenine dinucleotide (FAD): accepts ___ electrons plus ___ protons to form FADH2. | two; two |
| Nictoninamide adenine dinucleotide (NAD+) accepts __ electrons plus ___ proton to form NADH. | two; one |
| Adenosine triphosphate (ATP) is the energy currency for __. | cells |
| ___ provide the fuel for most cellular activities. | ATP |
| ATP --> ADP and P is a highly ___ reaction. | exergonic |
| Exergonic phosphorylation reactions are coupled to ___ reactions. | endergonic |
| ____ hydrolysis is the substrate level phosphorylation. | ATP |
| ATP hydrolysis directly adds a ___ group to another molecule. | phosphate |
| ATP hydrolysis changes a protein's ___ or increase ___. | shape; reactivity |
| Rates in an enzyme are increased by ___ and __. | heat and catalysts |
| Catalysts reduce ____ ___. | activation energy |
| Enzymes are protein __. | catalysts |
| true or false: Enzymes or catalysts are specific for each type of reaction. | true |
| ___ bind to the enzyme's active site. | substrates |
| In an enzyme substrate, many enzymes undergo a ____ change. | conformational |
| ___ fit: reactants brought together in precise orientations and strains bonds. | induced |
| __ lower the activation energy, therefore enzymes are not consumed during the reaction. | enzymes |
| The ___level is a plateau where nearly all active sites occupied by the substrate. | saturation |
| Vmax means what? | Velocity of reaction near maximal rate |
| ____ ___ occurs when a molecule competes with the substrate for the active site. | Competitive inhibition |
| ___ ___ occurs when a molecule binds at a location other than the active site. | Allosteric regulation |
| Allosteric regulation causes a change in the enzyme __. | shape |
| Allosteric regulation can activate or deactivate the ___. | enzyme |
| When regulating an enzyme, the regulation process may involve covalent modifications that can be ___ or not. | reversible |
| Phosphorylation causes a ____ change in shape and may activate or inactive the enzyme. | reversible |
| ___ pathways break down molecules. | catabolic |
| catabolic pathways are used for recycling, are ___ (release energy), and store in energy intermediates. | exergonic |
| ___ pathways synthesize molecules. | anabolic |
| Anabolic pathways promote ____ and are endergonic. | synthesis |
| What are some enzyme helpers? (list 2) | vitamin C and collagen |
| Vitamin B3 (Nicotinic Acid, function in the coenzymes NAD and NADP are all enzyme ___. | cofactors |
| Enzyme function is dependent on ___ and ___. | temperature and pH |
| ____ affects the folding and movement of the enzyme and its substrates. | temperature |
| ____ affects the enzyme's shape and reactivity. | pH |
| Carbohydrates are also known as __. | sugars |
| ___ play an important role in energy, contribute to cell structure, and are involved with cell recognition and identity. | carbohydrates |
| The molecular formula (CH2O)n belongs to ___. | carbohydrates |
| Carbohydrates are __ in water. | hydrophilic |
| What are the 3 main forms of carbohydrates? | Monosaccharides, Oligosacchardies, and Polysaccharides |
| How many sugars are in a monosaccharide monomer? | one |
| How many sugars are in a oligosaccharide small polymer? | few |
| How many sugars are in polysaccharide large polymers? | many |
| Monosaccharide are single ___. | monomers |
| Oligosaccharide are small ___. | polymers |
| Polysaccharide are large __. | polymers |
| ____ monomers are simple sugars that structurally vary. | Monosaccharide |
| What are the 4 primary ways that Monosaccharide monomers vary? | Location of the carbonyl group, number of carbon atoms, spatial arrangement of their atoms, and the linear alternative ring forms |
| When the carbonyl group is at the end, the ending is what? | aldose |
| Polypeptide bonds are formed by ___ ___. | dehydration synthesis |
| When the carbonyl group is in the middle, the ending is what? | Ketose |
| If there are 3 carbon atoms present, the simple sugar is ___. | triose |
| If there are 5 carbon atoms present, the simple sugar is ___. | pentose |
| If there are 6 carbon atoms present, the simple sugar is __. | hexose |
| Sugars typically form ring structure in ___ solutions. | aqueous |
| α-1,4-glycosidic linkage and β-1,4- glycosidic linkage are the two most common linkages of ____. | polysaccharides |
| Β-glycosidic linkages have ____ rings. | flipped |
| true or false: Β-glycosidic are not easily broken down by all organisms. | true |
| True or false: A-glycosidic linkages are easily broken down by all organisms. | true |
| Plants store ____ as starch. | sugar |
| ___ monomers can be used for energy. | glucose |
| Plant sugars form a __. | helix |
| Beta linkages are much harder to ___. | hydrolyze |
| What enzyme breaks down lactase? | Lactose |
| Animals store sugar as ___. | Glycogen |
| Sugar in animals is store in the ___ and ___ cells. | liver and muscle cells |
| ___ proteins and contractile proteins are responsible for moving the cell itself or moving large molecules. | motor |
| ___ is the basis for storing and processing genetic information that passes from one generation to the next. | DNA |
| An input of ___ is required to link amino acids and form proteins. | energy |
| ___ perform a variety of cell functions, including catalysis, defense, signaling, movement, transport, and structure. | proteins |
| The sickling seen in red blood cells with the defective hemoglobin subunit results from a change in the ____ _____ of _____. | primary structure of hemoglobin |
| In most proteins, ___ groups are aligned and form hydrogen bonds. | polar |
| On a chemical analysis, a particular protein was found to contain 438 amino acids. How many peptide bonds are present in the protein? | 437 |
| What bond type is responsible for the secondary structure of a protein? | Hydrogen |
| A ____ bond is a covalent bond formed via a condensation reaction. | peptide |
| Aspartate and glutamate are highly soluble in water because they have electrically charge side chains or ____ ___. | R-groups |
| Amino acids with _____ r-groups or side chains do not interact with water because their side chains are nonpolar. | hydrophobic |
| Nonpolar side chains lack ____ or highly electronegative atoms capable of forming hydrogen bonds with atoms. | charged |
| ___ cause changes in the shape of normal proteins that can lead to cell death. | Prions |
| R-groups that consist soley of carbon and hydrogen atoms rarley participate in ___ reactions. | chemical |
| R-groups that only contain carbon and hydrogen atoms are __. | nonpolar |
| _____ side chains lack charged or highly electronegative atoms capable of forming hydrogen bonds with water. | nonpolar |
| The R-group determines how ___ each amino acid is in water. | soluble |
| ___ do not serve as a good template for replication. | proteins |
| A ___ R-group would most likley be found buried in the interior of a protein. | hydrophobic |
| A chemical that breaks disulfide bonds might destroy the __ level of the protein strucutre. | tertiary |
Created by:
ehabel
Popular Biology sets