NWHU biochem exam 3
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| what is a peptidoglycan composed of | carbohydrate and a protein (peptide)
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| common information on glycoproteins | oligosaccharide attached to a protein, ommon in membrane proteins, for communication, blood type, hormones, antibodes, secreted proteins
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| What are the glycosidic bonds of oligosaccharide linkages | acetal, ketal, bonds between carb and amino acid r-group, bonds between carb and lipid
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| info on proteoglycans | polsaccharides connected to proteins, in connective issue, provides structure in extracellular matrix, growth factor activation, adhesion
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| info on glycolipids | in cytoplasmic membanes, used for blood types
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| what glycoconjugates are involved in communication relating to membranes | glycoprotein and glycolipid
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| what glycoconjugate is involved n functions of the extracellular matrix | proteoglycan
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| what are the functons of proteoglycan | storage of water, joint lubrication
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| what glycoconjugate is involved in the outer membrane of gram-negative bacteria | lipopolysaccharide
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| 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
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| where is the carbohydrate attached in a glycoprotein | to its anomeric carbon through a glycosidic link to the -OH
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| what specifically are proteoglycans | one or more large glycans, called sulfated glycosaminoglycans are covalently attached to a core protein
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| examples of glycosaminoglycans | heparan sulfate, chondroiin sulfate, dermatan sulfate, keratan sulfate
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| where are proteoglycans located | bound to the outside of the plasma membrane by a transmembrane peptide or a covalently attached lipid.
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| what do proteoglycans do | provide points of adhesion, recognition, and information transfer between cells, or between the cell and the extracellular matrix
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| 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
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| what is a common characteristic between cell surface, extracellular, and secreted proteins | they are all glycoproteins
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| 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
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| what is the sugar code | represents specific interactions between distinct oligosaccharides and receptors
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| 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
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| what are lectins | proteins with a ligand site that bind carbohydrates with high specificity and affinity.
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| 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)
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| where are lectins found | commonly found on the outer surface of cells
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| 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
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| 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
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| what is the purpose of intracellular lectins | they mediate intracellular protein targeting to specific organellesor the secretory pathway
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| do viruses bind to oligosaccharides through cell surface glycoproteins or glycolipids | glycoproteins, as the first step in infection
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| do bacterial toxins (cholera, pertussis)bind to oligosaccharides through cell surface glycoproteins or glycolipids before entering a cell | glycolipids
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| 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
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| 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
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| A deficiency in what vitamin leads to night blindness, blindness, or dry skin, eyes, and mucous membranes | Vitamin A (retinol)
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| What are general functions of vitamin A | pigment, hormone signalling
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| A deficiency in what vitamin leads to Beriberi, and what are the general functions of that vitamin | vitamin B1 (thiamine), coenzyme in central enzymes
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| What are the functions of vitamin B2 (riboflavin) | integral part of coenzymes (FAD, FMN) involved in energy production
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| 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
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| What are the general functions of vitamin B5 (pantothenic acid) | integral part of coenzyme A (acyl carrier, fat biosynthesis)
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| what are the general functions of vitamin B7 (Biotin) | coenzymes of carboxylases (add COO- from CO2)
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| what are the general functions of vitamin B6 (pyridoxine or pyridoxol; pyridoxal and pyridoxamine) | coenzymes of ~100 enzymes
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| 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)
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| 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
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| 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
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| 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
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| What are the general functions of vitamin E | Antioxidant, inhibits platelet aggregation, and enhances vasodilation
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| 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
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| What are the basic building blocks of a nucleotide | phosphate group, amino acid base, and and a pentose group
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| what is the pentose called in RNA, DNA | ribose, deoxyribose
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| what are the bonds beween the phosphate groups in a nucleotide, if there are more than one | anydride bonds (high energy)
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| what are the possible base types in the nucleotide | purine, pyramidine
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| what are the possible pyramidines, purines | pyramidines: cytosine, thymine (dna), uracil (rna) purines: adenine, guanine
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| 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
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| What are examples of the coenzymes of which nucleotides are a part | NAD+, FAD, coenzyme A
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| what are the bonds that link successive nueotides in nuceic acids | phosphodiester bonds
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| 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
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| 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
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| Who published the discovery of DNA, and when was it published | 1953 James Watson and Francis Crick
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| when was the Nobel prize awarded for the discovery, and to whom | 1962, Wason, Crick, and Maurice Wilkins
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| what are mutations in genes | inherited changes in the nucleotide sequence of DNA
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| 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
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| What hppens in deamination | loss of an amino group
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| what happens in depurination | purine-pentose bond breaks
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| what can happen as a result of UV radiation | Thymine dimer (DNA reads 2 adjacent thymines as 1, causes frame shift mutation)
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| 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
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| 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
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| What are lipids | water insoluble cellular components, can be extracted by nonpolar solvents
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| 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)
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| 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.
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| 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)
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| What does it mean for a hydrocarbon chain to be unsaturated | it contains no double bonds
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| 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)
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| what do storage lipids consist of | glycerol, 3 fatty acids
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| what are fatty acids with multiple double bonds called | polyunsaturated fatty acids
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| 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)
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| 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
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| which end of the fatty acid is counted first in PUFAs | the double bond furthest from the COO- is counted first
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| FA 16:0 | Palmitic acid, palmitate (product in fatty acid synthesis in humans)
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| FA 18:2delta9,12 | Linoleic acid (essential FA) omega-6
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| FA 18:3delta9,12,15 | alpha-linoleic acid (essential FA) omega-3
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| FA 20:4delta5,8,11,14 | arachidonic acid (precursor for inflammation) omega-6
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| FA 20:5delta5,8,11,14,17 | Eicosapentaneoic acid (precursor for regulatory compounds in inflammation) omega-3
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| FA 22:6delta4,7,10,13,16,19 | Docosahexaneoic acid, omega-3
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| where is triacylglycerol formed | in adipose tissue, in the liver (COO- bonds to the -OH of the glycerol backbone in a condensation reaction
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| 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
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| What are the 2 basic types of membrane lipids | glycerophospholipids, sphingolipids
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| what are characteristics of the lipid bilayer | two layers of hydrophilic heads with hydrophobic tails between them
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""""""""" tails
""""""""" tails
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| What is the meaning of amphipathic in terms of membrane lipids | one component is hydrophobic and another is hydrophilic
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| 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
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| where are common examples of ether-lipids | membrane lipids in cardiac muscle of the heart
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| 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)
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| what is another function of ether lipids | pregnancy (implantation of fertilzed egg, maturation of fetus, induction of labor)
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| good way to identify triacylglycerols | 3 ester bonds with fatty acids
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| good way to identify etherlipids | has an ether bond in the hydrophobic end
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| good way to identify a sphingolipid | has an amide bond and no additional hydrophilic group
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| good way to identify glycerolphospholipids | look for phosphoesters
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| what are some examples of lipids as signals and cofactors | hormone (steroid, paracrine- prostaglandines, thromboxanes, leukotrienes), coenzymes in e- transport-- quinones
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| what is ubiquinone | a mitochondrial electron carrier (coenzyme Q)
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| what are eicosanoids | substances that act only on the cells near the point of hormone synthesis-- not transported through the blood
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| what are eicosanoids derived from | arachidonic acid (20:4delta 5,8,11,14)
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| what are the three classes of eicosanoids, paracrine hormones | prostaglandins, thromboxanes, and leukotrienes
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| what are steroids | oxidized derivatives of sterols- many that perform anti-inflammatory activities
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| what are some characterisitics of the biological membrane | diameter of 5-8 nm, made up of phospholipids, proteins; flexibility; separation of compartments; selectively permeable
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| 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)
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| 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
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| 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
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| what does staph aureus do | releases alpha hemolysin subunits, aggregate in host form pores (multi subunit complexes)
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