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| bond that holds long polymers of L-amino acids together via the loss of a water molecule. Link the acid and amine groups of two amino acids. |
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| Cross-links two appropriately placed cysteines by oxidizing the sulfhydryl groups, creating disulfide bridge |
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| methyl ester derivative of aspartic acid and phenylalanine |
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| important neurotransmitter molecule involved in regulation of emotions; synthesized from L-tryptophan through 2 enzymes, which add a hydroxyl group and strip away the carboxylic acid group |
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| sodium salt of glutamic acid, present in nearly all protein foods (disproportionately in meats, cheese, and tomatoes) |
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| cannot be synthesized by body, including valine, leucine, isoleucine, phenylalanine, tryptophan, methionine, and threonine |
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| protein types that share a significant amount of sequence similarity but have different functions. |
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| type of secondary structure; extended helical coil in which each successive residue of the helix has the same set of backbone tortional angles, stabilized by series of hydrogen bond between carbonyl and N-H group, most common structural element, responsible for flexibility and extendability of wool fibers, hair |
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| : type of secondary structure; polypeptide chains are almost completely extended with hydrogen bonds forming between adjacent strands of the polypeptide, can be parallel or antiparallel, found in silk |
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| required for a protein to be globular, happens to occasionally produce a compact ball, four successive residues that reverse the direction of the chain, stabilized by hydrogen bond |
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| shows possible combinations (Φ & Ψ) that don’t produce steric overlaps |
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| major protein of connective tissue, has repetitive sequences of Gly-X-Y, contains many proline and lysine |
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| collagen has an ability to form gels; when collagen is heated in water, the triple helix unravels as the strands denature and become disordered. When cooled, chains will become entangled as portions of chains twist into short regions of the triple helix. Temperature depends on type and sequence. |
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| occurs when the conformation of a backbone chain is specified, which is simplified by a special feature of the peptide group. Partial double bond character of peptide bond inhibits rotations, force all (white) atoms to lie in the same plane |
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| process by which folded proteins lose their native conformation under nonphysiological conditions such as elevated temperatures, high concentrations of solutes (ura, guanidinium, thocynate) or nonphysiological pHs Hydrogen bonds break and it is more entropically favorable to unravel. |
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| principle protein of wheat flour, made up of gliaden (soluble in alcohol, little elasticity, act as plasticizer) and glutenin (insoluble, even in alcohol; cohesive and elastic) |
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| proteins found in cells that help newly synthesized protein chains fold properly to their native states but don’t determine the folding pattern. Necessary to prevent hydrophobic aggregation and precipitation of unfolded chains |
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| large beta sheet twists and coils to form a closed structure in which the first strand is hydrogen bonded to the last, arranged in an antiparallel fashion |
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| from Wikipedia, genetically engineered to have a gene knocked out and replaced with an artificial piece of DNA, which casues a change in phenotype of the mouse. Can be used as an animal model to determine the function of the knocked out gene |
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| the most abundant whey protein, typical globular protein, 4 genetic variants (A through D), structure varies by pH: below 3.5 – monomer, above 3.5 – noncovalent dimer, between 3.7 and 5.4 – octamer, above 5.4 – dimer, above 7.5 – monomer |
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| an oligosaccharide is covalently linked to side chains of protein. Example is k-casein. |
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| Highly polydisperse, made up of submicelles, average diameter is 25 nm. There exists a dynamic equilibrium between free casein and submicelles, dissolved and colloidal calcium and phosphate, and free submicelles and micelles |
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| what makes up the larger casein micelle, resemble true micelles because their behavior is assumed to be dominated by beta-casein components; have hydrophobic core and hydrophilic surface. Held together within the “Casein micelle” by hydrophobic forces and colloidal calcium phosphate clusters bridging the phosphate groups on different casein molecules. Aggregate by hydrophobic association |
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| heat the food sample, converting all organic nitrogen to ammonium sulfate, add sulfuric acid, which neutralizes the ammonium sulfate, and produces ammonia vapor, which is distilled and collected as an acid |
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| is especially promoted in the crust of bread (which has starch granules that do not gelantinize extensively in the outermost layer) because it is of low moisture, elevated temperature, and has reducing sugars available due to the action of amylases |
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| started in cattle, transmitted to humans. Occurred since world war II. |
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| fatal, degenerative, neurological disease, sort of resembles Creutzfeld Jacob disease |
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| “proteinacious infectious particle” it is unsure what they do but they are denaturing, serves as template for further denaturing for an autocatalytic response |
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| a sweet tasting protein, used as both flavor enhancer and sweetener, has licorice-like after taste. |
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| small protein complex from a West African fruit, has extended beta sheet made up of four antiparallel strands, with single alpha helix perpendicular to the direction of the sheet strands, significantly sweeter when you include arginine, heat stable to 98 |
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| found in small red berry of miracle fruit, has the ability to change perception of acid-triggered sourness to a strong, sweet taste. Dimer structure is required for sweet taste stimulation effect. Lasts for about ½ an hour. |
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| responsible for allergies, Ara 1-7 have been identified, part of the 2S protein? (335) |
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| taste described as meaty, associated with L-glutamic acid & MSG |
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| Water-soluble soy protein stored in small granules |
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| a blood serum protein that is also present in milk, contains nearly 300 soluble proteins including antibodies, proteases, and protease inhibitors. IgM acts as an agglutin by precipitating onto fat globules at low temperatures |
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| “the stiffness of death” muscles are locked into a contracted state as cellular respiration stops and mitochondria run out of energy, unable to generate further ATP (BECAUSE THE ANIMAL IS FREAKING DEAD) to pump calcium against gradient, myosin binds to actin but it cannot be removed, so muscles are contracted. |
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| lipoproteins that make up the largest fraction of yolk proteins, lipid and metal storage proteins |
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| makes up 12-13% of albumen protein, homologus to transferrin, which binds and transports ferric iron. Can bind Fe, Mn or Cu. Also called ovotransferrin. Has the lowest denaturation temperature, so it determines at which temperature egg whites become “white” |
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| most abundant of albumen proteins, has four cysteine residues but only one disulfide bond with two unpaired, reactive sulfhydryl groups. Phosphorylated with 2 phosphate groups, is trypsin inhibitor, weakly foaming agent and resistant to surface denaturation, somewhat resistant to heat denaturation |
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| carcinogenic compound that occurs when (Secondary??) amines produce nitrogen gas and hydroxide by deamination |
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| enzyme present in saliva, tears, egg white, and other body fluids that can destroy cell walls of bacteria and act as a mild antiseptic. Also called muramidase. |
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| a highly reactive amino acid that can react with nucleophilic groups (amines, thiols) of other amino acid side chains to form cross links within or between proteins |
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| major storage protein in corn kernels, occur in endosperm of maize, hydrophobic in water but soluble in alcohol. Present as nitrogen storage for developing embryo. Poor source of lysine, tryptophan. |
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| Hydrolyzed vegetable protein |
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| a mixture of free amino acids and short polypeptides produced by treating soy, maize, and wheat protein with acid at a high temperature |
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| same process of HVP, but exclusively a soy product |
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