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
BCH 4053
Final Exam Concepts
| Term | Definition |
|---|---|
| primary structure | the amino acid sequence of a protein |
| secondary structure | local arrangement of the protein in regards to alpha helices and beta sheets |
| tertiary structure | the 3D folding a protein into its final form |
| quaternary structure | when multiple tertiary structures come together to form a multi-subunit protein |
| consensus sequence | the calculated order of most frequent residues found at each position in a sequence alignment |
| protein domains | sections of a protein that can function independently if they were to be cleaved off |
| chaotropic agents | a molecule in water solution that can disrupt the hydrogen bonding network between water molecules |
| hydrophobic collapse | the early stage of protein folding that takes only 5 ms |
| molten globule | much of the secondary structure of the native protein but little of its tertiary structure |
| folding funnel | assumes that a protein's native state corresponds to its free energy minimum under the solution conditions usually encountered in cells |
| Bohr effect | hemoglobin's oxygen binding affinity is inversely related both to acidity and to the concentration of carbon dioxide. |
| allosteric regulation | the regulation of a protein by binding an effector molecule at a site other than the protein's active site. |
| symmetry model of allosterism | postulates that enzyme subunits are connected in such a way that a conformational change in one subunit is necessarily conferred to all other subunits |
| sequential model of allosterism | holds that subunits are not connected in such a way that a conformational change in one induces a similar change in the others. Thus, all enzyme subunits do not necessitate the same conformation; substrates bind via an induced fit protocol. |
| lock and key model | both the enzyme and the substrate possess specific complementary geometric shapes that fit exactly into one another |
| induced fit model | only the proper substrate is capable of inducing the proper alignment of the active site that will enable the enzyme to perform its catalytic function |
| prosthetic group | A permanently associated coenzyme |
| epitope | the part of an antigen that is recognized by the immune system |
| paratope | the part of an antibody which recognizes an antigen |
| antigen | any structural substance which serves as a target for the receptors of the immune system |
| transition state analogs | chemical compounds with a chemical structure that resembles the transition state of a substrate molecule in an enzyme-catalyzed chemical reaction |
| cofactor | metal ions |
| coenzyme | small organic molecules |
| reaction molecularity | the number of colliding molecular entities that are involved in a single reaction step |
| reaction order | the index, or exponent, to which its concentration term in the rate equation is raised. |
| therapeutic index | a comparison of the amount of a therapeutic agent that causes the therapeutic effect to the amount that causes toxicity. |
| lead compound | used as a starting point to design even more efficient drug candidates. |
| clinical trial phases | Phase I assesses the safety and tolerability of a drug. Phase II tests the efficacy of a drug candidate against the target disease and to assess dosing requirements. Phase III confirms the efficacy of a drug candidate and monitor its long-term effects. |
| double blind test | neither subjects nor doctors know which group of patients receive the drug candidate or control compounds |
| integral proteins | hydrophobic and are immersed into the lipid bilayer |
| peripheral proteins | connected to the surface of the lipid bilayer |
| lipid-linked proteins | membrane-associated proteins that contain covalently linked anchoring lipid molecules. |
| membrane skeleton | maintains the shape of the cell and is important for cellular motion, intracellular transport and cellular division. |
| lipid rafts | considered to be organizing centers for the intracellular signaling system. |
| intrasteric regulation | the binding of Ca2–CaM to this peptide segment extracts the autoinhibitor from MLCK’s active site, thereby activating the enzyme |
| membrane potential | the difference in electric potential between the interior and the exterior of a biological cell. |
| action potential | a short-lasting event in which the electrical membrane potential of a cell rapidly rises and falls, following a consistent trajectory. |
| receptor desnitization | decreasing the response to a signalling molecule when that agonist is in high concentration |
| fluid mosiac model | the components of the plasma membrane are able to move laterally or sideways throughout the membrane |
| signaling peptide | a short peptide present at the N-terminus of the majority of newly synthesized proteins that are destined towards the secretory pathway |
| high energy compounds | molecules with bonds that are hydrolyzed with large negative values of  deltaG |
| oxidoreductases | catalyze redox reactions (transfer of e- or H atoms); ex: NAD+, NADP+, FAD, FMN |
| transferases | catalyze the reactions of functional group transfer; ex: acetyltrasferases |
| hydrolases | catalyze hydrolysis reactions; ex: peptidases, ATPases |
| isomerases | catalyze the interconversion between isomers; ex: racemaes, toposiomerases |
| ligases | catalyze the joining of two large molecules, which is usually accompanied by hydrolysis of ATP; ex: DNA ligase |
| lyases | catalyze the non-hydrolytic cleavage of chemical bonds or the addition of groups (often water) to double bonds; ex: decarboxylase |
| chymotrypsin | FYW, unless followed by P; pH=8 |
| trypsin | RK, unless followed by P; pH=8 |
| endopeptidase V8 | E; pH=8 |
| elastase | VAGS, unless followed by P; pH=8.5 |
| competitive inhibition | Km(app) increases; crosses the non-inhibitor line at the y-axis |
| uncompetitive inhibition | Km(app decreases; V(max) decreases; parallel to non-inhibitor line |
| mixed (non-competitive) inhibition | V(max) decreases; crosses the non-inhibitor line to the left of the y-axes |
| A DNA | pitch of 2.5 nm; 11 bp/turn |
| B DNA | pitch of 3.4 nm; 10.5 bp/turn |
| uniporter | moves only one molecule in one direction; ex: GLUT1 |
| symporter | moves two molecules in one direction; ex: SGLT1 |
| antiporter | moves two molecules in opposite directions; ex: Na/K pumps |
Created by:
JacobGant
Popular Biochemistry sets