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Micro Test 3
| Question | Answer |
|---|---|
| what are the 3 components of a nucleotide (subunit of a nucleic acid)? | 5 carbon sugar, phosphate group, and nitrogenous base unit |
| what is DNA composed of (2 things)? | deoxyribose and its sugar |
| what are the 4 bases associated with DNA? | adenine, thymine, guanine, and cytosine |
| the backbone of DNA is a repeat of what? | sugar and phosphate group to which nucleotides are attached |
| what part of the backbone do the bases extend from? | the sugars |
| what type of bonds link the bases? | hydrogen bonds |
| what happens during transcription? | the base units of RNA nucleotides pair up with corresponding base unit of DNA and uracil replaces thymine |
| What are the 3 types of RNA (full name) | messenger RNA, transfer RNA, and ribosomal RNA |
| what is the function of the mRNA? what is it broken into? | it carries information from part of the DNA and acts as a blueprint for the protein. it is broken into codons |
| what is the sense strand? | the strand of DNA that is copied |
| what is the function of the rRNA? Where is it transcribed from? | it forms the framework of the ribosome which is where translation takes place. it is transcribed from rRNA genes on DNA |
| where does the transfer RNA take anticodons from and where do they go? | from the cytoplasm to the ribosome |
| how many different types of tRNA are there? | 61 to correspond with the 61 codons |
| what does the codon AUG code for? what chamber is this first codon located in? | methionine. the P site |
| the left and right side chambers are called what respectively? | left: P site right: A site |
| what are the 4 parts of a protein? | central carbon, amine group (NH2), carboxyl group, and a radical group |
| what differentiates one protein from the next? | the radical group |
| what is the primary structure of a protein? what does this structure look like? | sequence of amino acids within protein, this structure is linear |
| secondary structure of a protein? what 2 d structure is formed and how is this further elaborated on? | folding of a molecule created by bond angles and the 2 d version created a pleated sheet, and the twisting of this sheet forms an alpha helix |
| tertiary structure of a protein? what bonds link this structure? | 3D structure where alpha helix coils on itself and disulfide bonds covalently link adjacent amino acids |
| Quaternary structure | a functioning protein has subunits that each has primary, secondary and tertiary structures |
| isoenzymes | enzymes with different levels of functioning that are varied by their subunits (of the overall protein) |
| what are point mutations? | changes in a single base unit in sequence which can either result in intended protein or a different ne depending on what is changed |
| microevolution is caused by what and what is it? | a point mutation in the codons create a protein that is more or less efficient than the original one. if it is beneficial and improves functioning and thus survival, it can be passed to offspring |
| what are the two kinds of frameshift mutations? What happens? | addition and deletion. the insertion or deletion of a nucleotide causes everything to shift left or right by one, everything past this wrong nucleotide is then messed up by 1 and will code for wrong protein |
| addition? | a nucleotide inserts itself into sequence |
| deletion? | a nucleotide removes itself from sequence |
| define an enzyme? what type of macromolecule is it? | a catalyst in a living system that overcomes activation energy needed to start a reaction. it is a protein |
| What are the three components of an enzyme? | a protein, a cofactor and a conezyme |
| what is a cofactor typically composed of? | a metallic ion |
| what is a coenzyme typically composed of? | a vitamin |
| What is the active site of an enzyme likened to? | a keyhole |
| what are the three requirements for an enzyme to activate a substrate? | specificity (fit into active site), orientation (activation sides are facing each other), and active sites match |
| what is compound specificity? what is an example? what is the drawback? | similar compounds can be acted on by a single enzyme. an example is glucose, galactose and fructose being able to be acted on by the same enzyme, however the drawback is that it is not as efficient because it cannot fit snugly to be able to activate all 3 |
| what is group specificity? what is an example? | only one group fits into the active site and the rest of the molecule is outside of active site. examples are active sites that accept amine or carboxylic acid groups |
| what is linkage/ bond specificity? what is an example? | only a single bond can be broken and it will not otherwise break the bond. an example is pepsin (breaks down enzymes) which only breaks peptide bond between adjacent phenylalanine molecules |
| what parts does a holoenzyme have? | core protein and cofactor |
| what is an apoenzyme? what does it form? | just a core protein and thus an inactive enzyme, which when combined with a coenzyme/cofactor forms a holoenzyme |
| how does a competitive inhibitor work? is it reversible? | it mimics a substrate and fit into the active site, because it fits all requirements except having a matching activation site. it is reversible |
| how does a non-competitive inhibitor work (2 types)? is it reversible? give examples for the first one? | it either completely inhibits the enzyme by acting like a key that broke in a lock (irreversible) or uses an allosteric enzyme with a secondary site to block active site. an example of the first is arsenic and cyanide |
| how does an allosteric enzyme work? | a secondary site has an effector/modulator which fits into it and either inhibits or facilitates a reaction |
| positive allosteric enzyme works how? | the effector fits into the secondary site and this resulting shape opens the active site to work properly and the reaction proceeds |
| how does a negative allosteric enzyme work? | the effector fits into the secondary site and the resulting form inhibits the active site |
| what is feedback control? why does this happen? | in a series of reactions, a later material that is produced feeds back to an earlier reaction to inhibit it for a period of time. this happens because many reactions happen at different speeds |
| what are constitutive proteins/enzymes? | proteins that are always needed and thus always made |
| what are adaptive or inducible proteins | proteins that are only made when they are needed |
| how is regulation enacted on transcription | the amount of mRNA is limited |
| how is regulation enacted at translation | the amount of protein is regulated |
| what does the operator do? what is it? | it is a control gene and length of DNA which serves as the binding site for the repressor. |
| regulatory gene | length of DNA that contains information from which repressor is made |
| what is the promoter? what does it initiate? | the point at which RNA polymerase binds and begins functioning to initiate transcription |
| what is the job of the inducer and what is it made of? what binds to it? | the inducer is a substrate which is bound to the repressor, because the repressor can only bind with one thing, the repressor leaves the operator open and transcription can take place |
Created by:
Lyd543
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