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MCB 3020
Exam 1
| Term | Definition |
|---|---|
| microbiology | the study of microorganisms and their activities |
| industrial microbiology | conversion of raw materials into desirable end products by selected microorganisms (large scale) |
| primary metabolites | production of products necessary for microbial growth like amino acids, organic acids, alcohol, certain enzymes, etc. |
| secondary metabolites | production of products by the microorganisms not necessary for its growth like antibiotics, steroids, ethanol, etc. |
| genetic engineering technology | applying gene technology or recombinant DNA technology do develop products by transferring defined genes into rapidly growing microorganisms (in vivo) |
| biotechnology | uses genetically modified microorganisms to synthesize products of high commercial value |
| bioremdiation | the use of living organisms to degrade pollutants in the environment |
| invariant structures of a cell (all cells have this) | cell membrane, ribosomes, DNA, RNA |
| variant structures of a cell (only certain cells have this) | cell wall, mitochondria, chloroplast, etc. |
| properties of all cells | metabolism, reproduction, and evolution. |
| characteristics of some cells | differentiation, communication, movement. |
| cells can be viewed as chemical machines (catalytic functions) | carry out chemical transformations within the confines ofa cellular structure using biological catalysts, enzymes |
| cells can be viewed as coding devices (genetic functions) | analogous to computers, which store and process genetic information (DNA) that is eventually passed on to offspring during reproduction. |
| origin of the earth | 4.6 BYA |
| origin of cellular life | 3.8 BYA |
| origin of oxygenation | 3 BYA due to cyanobacteria |
| origin of current oxygen levels | 500-800 MYA |
| Anton van Leeuwenhoek (1684) | first observation of bacteria |
| Jenner (1798) | introduces small pox vaccination |
| Pasteur (1864) | resolves the problem of spontaneous generation |
| Koch (1881) | grows pure culture of anthrax microorganism from cow postulates; developed the idea that a specific microorganism causes a specific disease. |
| 3 things needed for microbiology to develop as a science | (1) microscopy, (2) sterilization and aseptic techniques, (3) pure culture methods. |
| Resolving power=diameter of small resolvable object | (wavelength)/(2*Aperture) |
| phylogeny | permits grouping of organisms based on the evolutionary lines of descent |
| taxonomy | groups organisms for convenience of laboratory study and hence focuses on phenotype differences |
| Linean System | placed into either animalia (motile, nonphotosynthetic) or plantae (nonmotile, photosynthetic); invention of microscope forced rethinking; Darwin predicted transition types between the two groups |
| Haeckel System | placed into animalia, plantae, or protista( distinguished from the others by its relatively simple structure aka what didn't fit into the other two was placed here) |
| Haeckel's Prostia | unicellular (or if multi they do not develop differentiated tissues) included algae, fungi, protozoa, and bacteria (including blue-green "algae" aka cyanobacteria) |
| Haeckel's subdivision of Protista | higher protista (eukaryotic cell structure) cells similar to those of higher plants and animals and included algae, protozoa, and fungi. lower protista (prokaryotic cell structure) a simplified cell structure that included cyanobacteria and bacteria |
| eukaryotes | cellular organisms having a membrane bound nucleus where the genome is stored |
| Whittaker's 5 Kingdoms | monera (prokaryotic and unicellular includes bacteria, cyanobacteria) protista (eukaryotic and unicellular includes algae and protozoa) [the following are eukaryotic and multicellular] plantae (photosynthesis) fungi (absorption) animalia (ingestion) |
| Woese's 3 Domains | understanding relationships via ribosomal RNA that led to bacteria (all prokaryotes) archaea (all prokaryotes) and eukarya (all eukaryotes) |
| simple stain | dyes all cells the same color and does not differentiate between cells. lets you see the shape of the cell |
| negative stain | stains the background so that you can see the size of the microorganism |
| gram postive | look purple; thick peptidoglycan layer that doesn't let the dye leave easily |
| gram negative | look pink; thin peptidoglycan layer that easily lets dye leave |
| structural stains | spore [clostridium] (g+, anaerobic rod), capsule [bacillus] (g+, aerobic rod), and flagellum [sporosarcina] (coccus) |
| cultural characteristics | macroscopic appearance of growth in broths or deeps or on slants or streak plate. |
| biochemical and physiological properties | (enzyme level) where most classification is done |
| prokaryotic cells | average size is 1 micro meter in diameter |
| viruses | dna or rna (exception is mimivirus which has both). protein coat. |
| viroids | only rna. no protein coat. |
| prions | only protein. no protein coat. |
| GC/AT ratios of DNA | the higher the ratio, the higher the boiling point and thus the more stable the molecule is because GC forms 3 hydrogen bonds whereas AT only forms two. |
| phosphate | (PO4)^3- where one oxygen is double bonded to the phosphate and the rest of the oxygens are single bonded with negative charges. |
| van der waals forces | at very short distances any two atoms show a weak bonding interactions due to their fluctuating electrical charges; however, if they're too close together, they repel each other very strongly. |
| hydrogen bonds | when a hydrogen atom is sandwiched between two electron-attracting atoms (usually oxygen or nitrogen) |
| weak chemical bonds | player the bigger role in biological structures than strong chemical bonds. |
| hydrophobic forces | water forces hydrophobic groups together in order to minimize their disruptive effects on the hydrogen-bonded water network. |
| purine | two fused rings (Guanine and Adenine) |
| primidine | single ring (Cytosine and Thymine[DNA]) or Uracil (RNA) |
| what's in a cell? | 70% water and 30% chemicals(96% of that is macromolecules) |
| carbohydrates | organic compounds containing carbon, hydrogen, and oxygen in a ratio of 1:2:1. the most biologically relevant contain 4,5,6 carbon sugars (monosaccharides) |
| polysaccharides | carbohydrates containing many monomeric (sugar) units connected by covalent bonds known as Glycosidic bonds. two sugars joined by a glycosidic bond=disaccharide; addition of one more sugar=trisaccharide; addition of several more=oligosaccharide; |
| carbohydrate linkage | alpha orientation: glycogen and starch. beta: cellulose; however, they are comprised solely of glucose units but their functional properties are entirely different because of their configurations. |
| lipids | includes triglycerides, waxes, sterols, and fatty acids. non-polar that are solvable in non-polar solvents. fatty acids contain both a highly hydrophobic and hydrophilic (carboxylic acid head) regions. |
| phospholipids | two moles fatty acid and one mole phosphate esterified to glycerol |
| nucleotides | building blocks of nucleic acids that are composed of three nits: 5 carbon sugar, either ribose (in RNA) or deoxyribose (in DNA), a nitrogen base, and a molecule of phosphate (PO4)^3- |
| nucleic acids | backbone (polynucleotide) is a polymer in which sugar and phosphate molecules alternate; contains nucleotides covalently bonded via phosphate from Carbon 3' of one sugar to Carbon 5' of the adjacent sugar; phosphate linkage is called phosphodiester |
| DNA helix | is antiparallel in that one strand runs 5' to 3' whereas the other strand runs 3' to 5'; polymerase that replicates DNA only synthesizes 5' to 3' by copying the 3' to 5' strand. |
| DNA | deoxyribonucleic acid that carries the genetic blueprint for the cell; double stranded; stabilized by hydrogen bonds and hydrophobic base stacking. |
| RNA | ribonucleic acid that acts an intermediate to convert the blueprint to the amino acid sequence for proteins; single stranded; crucial as messenger, transfer, and ribosomal RNA; may have secondary structure due to hydrogen bonding |
| DNA base pairing | guanine (G) bonds with cytosine (C); adenine (A) bonds with thymine (T). |
| amino acids | monomeric units of proteins that where most consist of only hydrogen, oxygen, and nitrogen; all amino aids contain a carboxylic acid and an amino group; can be acidic ionizable, basic ionizable, non-ionizable polar; or non-polar. |
| peptide bond | HN-C=O; the carbon of the carboxyl group of one animo acid and the nitrogen of the amino group of a second amino acid |
| isomers | molecules with the same molecular formula but exist in different structural forms |
| enantiomers | have the same molecular and structural formulas, except that one is a mirror image of the other (can't be superimposed) |
| in most biological systems, the predominate isomers are: | L-amino acids and D-Sugars. |
| proteins | polymers of amino acids covalently bonded by peptide bonds; there are 2 types of proteins: enzymes and structural two amino acids=dipeptide; three amino acids=tripeptide; many amino acids=polypeptide; |
| primary structure | specific linear sequence of amino acids held together by covalent peptide bonds |
| secondary structure | interactions between parts that make up the polypeptide backbone; major elements: alpha helix and hydrogen bonded beta pleated shets |
| tertiary structure | overall conformation within a single polypeptide chain stabilized primarily by weak interactions folding in 3D space; van der waals, hydrogen bonding, ionic, and hydrophobic weak forces; only possible covalent is disulfide bridge. |
| quaternary structure | proteins consisting of multiple polypeptides; manner in which they associate. |
| alpha helix | oxygen and nitrogen atoms from different amino acids become positioned close enough in the twisted structure to allow for hydrogen bonding to occur |
| beta-sheet | the chain of amino acids in the polypeptide folds back and forth upon itself (instead of forming a helix) when the oxygen and nitrogens of the backbone are fully hydrogen bonded. The R groups are alternating above or below the plane. |
| denaturation | proteins and polypeptide chains that are exposed to extremes of heat, pH, chemicals, or metals will affect their foldings. it retains its primary structure (because it is held together by peptide bonds) but loses its secondary and quaternary. can refold. |
Created by:
JacobGant
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