Diagram of Essential Amino Acid Lysine ● ● Lysine is a base Physical properties: Polar‚ positively charged ● ● ● Highly reactive Hydrophilic Solubility: ^ soluble in cold water ● ● Reactivity: 0 Flammability: 1 (may be combustible at high temps Protein Structure Dehydration Hydrolysis Stabilizing Forces 1) Hydrophobic Interactions Non polar amino acids (leucine and phenylalanine are two examples). Weakest type of bond. 2) Hydrogen bonds: Polar or charged amino acids (example Tyrosine)
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Amino acid present in the lumen of the small intestine The goal is to cross through the epithelial cell membrane to enter into the epithelial cell’s cytoplasm – its charged cuz of side chains To get through the membrane the amino acid must cross the Simple columnar epithelial cells lining the apical surface of the small intestinal tract. These cells are impermeable to any harmful bacteria that may be ingested by the body‚ but permeable to necessary ions. Absorption of amino acids occurs
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The reaction between alpha-amino acid and ninhydrin involved in the development of color are described by the following five mechanistic steps: alpha-amino acid + ninhydrin ---> reduced ninhydrin + alpha-amino acid + H2O alpha-amino acid + H2O ---> alpha-keto acid +NH3 alpha-keto acid + NH3 ---> aldehyde + CO2 Step (1) is an oxidative deamination reaction that removes two hydrogen from the alpha-amino acid to yield an alpha-imino acid. Simultaneously‚ the original ninhydrin is reduced
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identify an unknown amino acid. IntroductionAmino acids are simple monomers which are strung together to form proteins. Amino acids play a key cellular role in structure and function. Proteins themselves participate in nearly every physiological event in the cell. Since all amino acids contain at least one amino and one carboxyl group‚ they are classified as amphoteric substances (meaning that they can act as either an acid or as a base) (1). Treating the zwitterion with acid will result an addition
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for Intact proteins and protein hydrlysates (at least tripeptide‚ 2 peptide bonds Result Pink to violet blue color Ninhyrin Test 1‚2‚3-indanetrione monohydrate or triketohydintene hydrate‚ ethanol Alpha- amino group (usually a general test for amino acids) Xanthoproteic Test Conc. HNO3‚ conc. NaOH For W‚F‚Y (aromatic except for H) Blue to blue-violet Oxidative decarboxylation color & deamination followed by (proline:hydroxypr condensation oline gives a yellow
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Essential Fatty Acids (EFAs) are fats that are required by the human body‚ but cannot be made by the body; therefore they must be obtained from external forces such as food. EFAs are the building blocks of all fats and oils and are required for both metabolic processes and for fuel. EFAs form the main component in the fats carried in our blood stream (triglycerides)‚ fats stored in our bodies and of cell membranes (phospholipids). (Erasmus‚ 1993)‚ (Wikipedia‚ Essential Fatty Acids‚ 2012) Two fundamental
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the RNA bases that are complementary to the DNA template strand that uses uracil opposite to adenine. The RNA polymerase which is an enzyme that moves from the 3’ to 5’end on DNA template strand to synthesis mRNA from 5’ to 3’. b. What is the amino acid sequence produced by translation of the mRNA sequence?
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experiment was to compare how side chains alter the ionizability of our three amino acids: alanine‚ aspartic acid‚ and cysteine. More specifically‚ we wanted to observe how a thiol group and a carboxyl group affected the ionizability of the rest of the amino acid. Because alanine contains a single methyl group on its side chain‚ we can easily compare the functional groups of aspartic acid and cysteine to it because both aspartic acid and cysteine start their side chains with a methylene group and then go
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is held up by a chain of subunits called amino acids that are connected by peptide bonds. Protein structures are formed by four levels of folding. The primary structure is the linear sequence of amino acids. The secondary structure describes the folding of alpha helixes and beta pleated sheets. The tertiary structure represents the overall shape of the protein and the quaternary structure only occurs in a protein consisting of more than one amino acid chain. When the shape‚ the structure or
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and these comprise only 20 kinds of amino acids in various combinations. These 20 kinds of amino acids are essential to the body. In addition to being the materials for proteins‚ they are used as an energy source for the body as necessary. Further‚ each amino acid plays an important and unique role in the body. The list below shows the role of each amino acid. | Valine Leucine Isoleucine | All of these 3 amino acids are called branched chain amino acid(BCAAs). They perform the important functions
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