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![Match the property with the amino acid.
Glutamic Acid
Glutamate
✓ [Choose ]
Proton Withdrawing
Proton Donating
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- Why is the reaction rate low at pH7? Be specific and say something about the enzyme structure at the molecular level!Color Reactions of Intact Protein: 1ml of water and 0.5 g of casein 1ml of water and 0.5 g of bean protein 1ml of water and 0.5 g of glutenDraw the amino acid cysteine (R = CH2SH) at pH 7.
- Function of citric acid? Give me handwritten answer with explaination?Which of the amino acid side-chains would you expect to be protonated (i.e. has not lost its proton) under neutral pH conditions? Include reasons supporting your prediction.cephalin phospatidyl ethanolamine Yields 2 fatty acids, phosphoric acid, glycerol, and choline upon hydrolysis Yields 2 fatty acids, phosphoric acid, glycerol, annd serine uponn hydrolysis
- Can u help me to explain to me, please? I stuggled. I don't understand The a-ketoglutarate that is produced inthe reaction is now free to accept a new quaternary ammonium group from another amino acid in a transamination reaction.Phosphorylated molecules with high _____________ values of hydrolysis have large phosphoryl group transfer potentials.30. Which is NOT a feature of a fatty acid? Even numbers of carbon atoms Can be saturated or unsaturated Straight chain with no branching Double bonds can be conjugated
- Starting from glutamine, glycine, aspartate, N 10-formyi-THF, how many ATP- equivalents are required for purine nucleotide synthesis? 2 8 4 6draw all the structures of the tribasic amino acid lysine involved in the equilibrium reactions that would take place during titration against NaOH, starting with the fully protonated form below (draw the R-group in full). H;N+- CH - COOH (CH2)4 NH3+Which one is the most likely to be a catalytic triad of an enzyme that follows general acid base catalysis? -Glu-His-Cys -Leu-His-Ser -Glu-Phe-Ser -Asp-His-Ala