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Biochem test 3-NW
NWHU biochem exam 3
| Question | Answer |
|---|---|
| what is a peptidoglycan composed of | carbohydrate and a protein (peptide) |
| common information on glycoproteins | oligosaccharide attached to a protein, ommon in membrane proteins, for communication, blood type, hormones, antibodes, secreted proteins |
| What are the glycosidic bonds of oligosaccharide linkages | acetal, ketal, bonds between carb and amino acid r-group, bonds between carb and lipid |
| info on proteoglycans | polsaccharides connected to proteins, in connective issue, provides structure in extracellular matrix, growth factor activation, adhesion |
| info on glycolipids | in cytoplasmic membanes, used for blood types |
| what glycoconjugates are involved in communication relating to membranes | glycoprotein and glycolipid |
| what glycoconjugate is involved n functions of the extracellular matrix | proteoglycan |
| what are the functons of proteoglycan | storage of water, joint lubrication |
| what glycoconjugate is involved in the outer membrane of gram-negative bacteria | lipopolysaccharide |
| what are characteristics of lipopolysaccharides | recognized by human immune system, variations of building blocks in polysaccharides lead to different serotypes, lipid A acts as toxin gets a reaction from the immune system |
| where is the carbohydrate attached in a glycoprotein | to its anomeric carbon through a glycosidic link to the -OH |
| what specifically are proteoglycans | one or more large glycans, called sulfated glycosaminoglycans are covalently attached to a core protein |
| examples of glycosaminoglycans | heparan sulfate, chondroiin sulfate, dermatan sulfate, keratan sulfate |
| where are proteoglycans located | bound to the outside of the plasma membrane by a transmembrane peptide or a covalently attached lipid. |
| what do proteoglycans do | provide points of adhesion, recognition, and information transfer between cells, or between the cell and the extracellular matrix |
| where are glycolipids and glycopolysaccharides located in the cell | components of the cell envelope, have covalently attached oligosaccharide chains exposed on the cell's outer surface |
| what is a common characteristic between cell surface, extracellular, and secreted proteins | they are all glycoproteins |
| what effect do the oligosaccharides have on the glycoproteins | they influence the folding and stability of the proteins, provide critical information about the targeting of newly synthesized proteins, and allow for specific recognition by other proteins |
| what is the sugar code | represents specific interactions between distinct oligosaccharides and receptors |
| what are the reasons behind the large number of possibilities of oligosaccharides | large number of building blocks, few restrictions with respect to size, unrestricted branching, and alpha- or beta- connections combined with -OH in many positions |
| what are lectins | proteins with a ligand site that bind carbohydrates with high specificity and affinity. |
| What are the purposes of lectins | wide variety of cell-cell recognition, signaling, and adhesion processes and in intracellular targeting of newly synthesized proteins (they intiate interaction with other cells) |
| where are lectins found | commonly found on the outer surface of cells |
| what happens when oligosaccharide tags are read by lectins in vertebrates | they govern the rate of degradation of certain peptide hormones, circulating proteins, and blood cells |
| what do lectins have to do with bacterial and viral pathogens and some parasites | they adhere to their targets by the binding of lectins in the pathogens to oligosaccharides on the target cell surface |
| what is the purpose of intracellular lectins | they mediate intracellular protein targeting to specific organellesor the secretory pathway |
| do viruses bind to oligosaccharides through cell surface glycoproteins or glycolipids | glycoproteins, as the first step in infection |
| do bacterial toxins (cholera, pertussis)bind to oligosaccharides through cell surface glycoproteins or glycolipids before entering a cell | glycolipids |
| what is an example of a cell-cell interaction mediated by lectins in the plasma membrane of a cell | neutrophils with the endohelial cells of the capillary wall at an infection site |
| what is the function of the mannose 6-phosphate receptor (lectin of the trans golgi complex) | binds the oligosaccharides of lysosomal enzymes, targeting them for the transfer into the lysosome |
| A deficiency in what vitamin leads to night blindness, blindness, or dry skin, eyes, and mucous membranes | Vitamin A (retinol) |
| What are general functions of vitamin A | pigment, hormone signalling |
| A deficiency in what vitamin leads to Beriberi, and what are the general functions of that vitamin | vitamin B1 (thiamine), coenzyme in central enzymes |
| What are the functions of vitamin B2 (riboflavin) | integral part of coenzymes (FAD, FMN) involved in energy production |
| Dficiency in what vitamin could lead to Pellegra, and what are the general functions of that vitamin | vitamin B3 (niacin) , integral part of coenzymes NAD and NADP involved in energy production |
| What are the general functions of vitamin B5 (pantothenic acid) | integral part of coenzyme A (acyl carrier, fat biosynthesis) |
| what are the general functions of vitamin B7 (Biotin) | coenzymes of carboxylases (add COO- from CO2) |
| what are the general functions of vitamin B6 (pyridoxine or pyridoxol; pyridoxal and pyridoxamine) | coenzymes of ~100 enzymes |
| Deficiency of what vitamin could lead to macrocystal megalblastic anemia, and what are its general functions | vitamin b9 (folic acid), coenzyme that transfers C1 units (nucleic and amino acid metabolism) |
| deficiency of what vitamin could lead to pernicious anemia, megaloblastic anemia, and neurologic symptoms; and what are its general functions | vitmin B12 (cobalamin), a coenzyme of enzymes that transfer alkyl groups |
| The deficiency of what vitamin could lead to scurvy and fatigue, and what are its eneral functions | vitain C, synthesis of collagen antioxidant, synthesis of carnitine, metablism of cholesterol |
| deficiency of what vitamin could lead to rickets, and what are its general functions | vitamin D, Ca2+ levels in the blood, bone density, modulator of the immune system |
| What are the general functions of vitamin E | Antioxidant, inhibits platelet aggregation, and enhances vasodilation |
| deficiency of what vitamin could lead to delayed blood clotting and hemorrhaging, and what are its general functions | vitamin K, blood clotting, prevents calcification of soft tissue/ cartilage |
| What are the basic building blocks of a nucleotide | phosphate group, amino acid base, and and a pentose group |
| what is the pentose called in RNA, DNA | ribose, deoxyribose |
| what are the bonds beween the phosphate groups in a nucleotide, if there are more than one | anydride bonds (high energy) |
| what are the possible base types in the nucleotide | purine, pyramidine |
| what are the possible pyramidines, purines | pyramidines: cytosine, thymine (dna), uracil (rna) purines: adenine, guanine |
| what are the basic functions of nucleotides | building blocks for DNA or RNA synthesis, energy currency in biological systems (ATP), chemical links in hormonal signals, structural components of several coenzymes |
| What are examples of the coenzymes of which nucleotides are a part | NAD+, FAD, coenzyme A |
| what are the bonds that link successive nueotides in nuceic acids | phosphodiester bonds |
| What is the way to tell apart the 5' end from the 3' end in nucleic acids | 5' has the phosphate group, 3' has the -OH |
| What are the ways complementary strands of DNA are stabilized when they are bonded together | hydrogen bonds stabilize double stranded structure between strands, hydrophobic interaction stabilizes between adjacent bases within each strand |
| Who published the discovery of DNA, and when was it published | 1953 James Watson and Francis Crick |
| when was the Nobel prize awarded for the discovery, and to whom | 1962, Wason, Crick, and Maurice Wilkins |
| what are mutations in genes | inherited changes in the nucleotide sequence of DNA |
| What are the types of mutations, and examples of each | Spontaneous: deamination, depurination; external factors: radiation (UV, Xray, gamma ray), chemical: deaminating agents, oxidative agents |
| What hppens in deamination | loss of an amino group |
| what happens in depurination | purine-pentose bond breaks |
| what can happen as a result of UV radiation | Thymine dimer (DNA reads 2 adjacent thymines as 1, causes frame shift mutation) |
| What can happen as a result of ionizing radiation | covalent bonds break, rings in bases can open, can cause depurination, bonds in the backbone can break; reactive oxygen forces can form |
| What are possible chemical causes of mutations | deaminating agents, can lose the amine group, oxidative agents, can cause oxygen radicals, possibly alter the structure of biomolecules |
| What are lipids | water insoluble cellular components, can be extracted by nonpolar solvents |
| what are the various functions of lipids | membrane, energy storage, energy source, coenzymes or prosthetic groups, signal transduction, hormones (regulation, communication), pigments (retinal from beta-carotene) |
| what are fatty acids | hyrocarbon derivativesat aout the same oxidation state (very low) as the hydrocarbons in fossil fuels. The hydrocarbon chains range from 4 to 36 carbons in length. |
| What is the result of the low oxidation state of the hydrocarbons in fatty acids | the cellular oxidation creates a lot of energy (similar to controlled rapid burning of fossil fuels in an internal combustion engine) |
| What does it mean for a hydrocarbon chain to be unsaturated | it contains no double bonds |
| what is the method of nomenclature for unbranched fatty acids | FA, total # of carbons: number of double bonds (delta followed by position of the double bonds) ex; 20:2(delta9,12) |
| what do storage lipids consist of | glycerol, 3 fatty acids |
| what are fatty acids with multiple double bonds called | polyunsaturated fatty acids |
| what is the difference between cis- and trans- configurations of PUFAs | cis- are healthy (from plants and fatty fish, grass-fed beef), trans- are not as healthy (bacterial activity in meat from ruminating animals, human-developed process: partial hydrogenation) |
| what are the physical property comparisons of fatty acids | bigger hydrocarbon tail--less water soluble, higher melting point; more cis- double bonds--more water soluble, lower melting point |
| which end of the fatty acid is counted first in PUFAs | the double bond furthest from the COO- is counted first |
| FA 16:0 | Palmitic acid, palmitate (product in fatty acid synthesis in humans) |
| FA 18:2delta9,12 | Linoleic acid (essential FA) omega-6 |
| FA 18:3delta9,12,15 | alpha-linoleic acid (essential FA) omega-3 |
| FA 20:4delta5,8,11,14 | arachidonic acid (precursor for inflammation) omega-6 |
| FA 20:5delta5,8,11,14,17 | Eicosapentaneoic acid (precursor for regulatory compounds in inflammation) omega-3 |
| FA 22:6delta4,7,10,13,16,19 | Docosahexaneoic acid, omega-3 |
| where is triacylglycerol formed | in adipose tissue, in the liver (COO- bonds to the -OH of the glycerol backbone in a condensation reaction |
| What is the comparison of energy storage of carbs vs. fats | fats hav higher energy content per weight, each gram of glycogen has ~2 g of H2O associated, fts have insulating properties, glycogen is short-term storage that is quickly accessible, fats are long-term storage with a slow mobilization process |
| What are the 2 basic types of membrane lipids | glycerophospholipids, sphingolipids |
| what are characteristics of the lipid bilayer | two layers of hydrophilic heads with hydrophobic tails between them 000000000 heads """"""""" tails """"""""" tails 000000000 heads |
| What is the meaning of amphipathic in terms of membrane lipids | one component is hydrophobic and another is hydrophilic |
| what is the difference between sphingolipids and glycerophospholipids | gycerophospholipids have 3 ester bonds and aphosphate group, sphingolipids have an amide bond and no ester bonds |
| where are common examples of ether-lipids | membrane lipids in cardiac muscle of the heart |
| what are functions of ether lipids | platelet activating factor (regulatory function, in blood, promotes blood clotting, released by white bood cells), functon of immunity (release of serotonin, upregulation of inflammation, allergic reactions) |
| what is another function of ether lipids | pregnancy (implantation of fertilzed egg, maturation of fetus, induction of labor) |
| good way to identify triacylglycerols | 3 ester bonds with fatty acids |
| good way to identify etherlipids | has an ether bond in the hydrophobic end |
| good way to identify a sphingolipid | has an amide bond and no additional hydrophilic group |
| good way to identify glycerolphospholipids | look for phosphoesters |
| what are some examples of lipids as signals and cofactors | hormone (steroid, paracrine- prostaglandines, thromboxanes, leukotrienes), coenzymes in e- transport-- quinones |
| what is ubiquinone | a mitochondrial electron carrier (coenzyme Q) |
| what are eicosanoids | substances that act only on the cells near the point of hormone synthesis-- not transported through the blood |
| what are eicosanoids derived from | arachidonic acid (20:4delta 5,8,11,14) |
| what are the three classes of eicosanoids, paracrine hormones | prostaglandins, thromboxanes, and leukotrienes |
| what are steroids | oxidized derivatives of sterols- many that perform anti-inflammatory activities |
| what are some characterisitics of the biological membrane | diameter of 5-8 nm, made up of phospholipids, proteins; flexibility; separation of compartments; selectively permeable |
| what are some of the movements of membrane lipids | uncatalyzed transverse ("flip-flop", very slow), transverse diffusion catalyzed by flippase (fast) , uncatalyzed lateral diffusion (very fast, happens within layer) |
| What are the two types of amino acid r-groups | alpha helices (membrane spanning), beta barrels (produced by bacteria, gram negative in outer membrane, create pores |
| what are some characteristics of beta barrel membrane proteins | "ribbons" lining pores in membranes, ~7-9 amino acids to span membrane once, ~20 sections of beta-helical polypeptide for one pore |
| what does staph aureus do | releases alpha hemolysin subunits, aggregate in host form pores (multi subunit complexes) |
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cooandrew
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