The amino acid shown below has an ionizable side chain with a pka of 4.When this amino acid is in a more basic solution (i.e., pH 11), it would resemble ionizationstate Cand have a charge of -1HOOHNH₂lonization state ANH3lonization state CHOOHNH3+Ionization state BdybNH₂lonization state D

There are four types of biological macromolecules- proteins, nucleic acids, lipids and…

Answered: The amino acid shown below has an…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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At pH 7, tryptophan crosses a lipid bilayer at about onethousandththe rate of indole, a closely related compound: Suggest an explanation for this observation.
The side chain of acetyl-L-lysine-OMe has a pKa=10.5 and its acid-dissociation reaction is shown below. see attachment for Question D.
Identify what type of chemical interactions is involved in the following side chains of the peptide chain below: 3 H-Q 0-H 5. OH OH CH, 6. 9. 4. -- CH, 2. 200 CH, 12 CH CH, -NH,0-C 4 1. 15 3. CH.-OH O CH. 17 18 The following choices can be applied for the following type of chemical interactions. 20 21 Write: AB - if it is a salt bridge or ionic bond CD - if it's a H-bonding 23 24 EF - if it's a hydrophobic interactions GH - if it's a disulfide bond
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Why do proteins have the net charge they have at low pH’s relative to high pH’s
Which of the following criteria must be met for a side chain protecting group to be considered orthogonal to the backbone amine protecting group in SPPS? It should be soluble in water. It should react with HOBT it should be stable at conditions in which the backbone amine protecting group is labile it should be labile at conditions in which the backbone amine protecting group is labile
Based on our pka's table, pKa1 of -COOH group of Cys = 1.71 pKa2 of -NH2 group of Cys = 10.78 pKa3 of side chain group of Cys = 8.33 If pKa is different, will the buffer change??
"Potassium Bromate (KBr03) is added to flour as a softener that strengthens the texture of bread. It can do this by forming disulfide bonds between two cysteine amino acids in a reaction similar to the chemical equation given below. The function of KBr03 is to remove the 2 electrons needed to form the disulfide bond as shown in the figure below. Each of the cysteine amino acids will be in a protein chain, so the reaction binds the two chains together, giving the dough cohesion. However, potassium bromate is a proven carcinogen and is only allowed in foods in the United States because bakers will add the right amount and correct It has been assumed to meet the temperature and cooking time conditions. " KBRO, + C,H¸NO,SH → KBr + H,O+C,H„N,O,S, Balance the reaction of potassium bromate (KBr03) with the cysteine molecule (C3H6 NO2 SH) by converting it into the reduced step matrix using the additive matrix method. (Kis the symbol of potassium in the question) (Homogeneous linear equation…
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An appropriate biochemical buffer should have charges in both its conjugate acid and conjugate base form. This avoids the presence of a neutral form of the buffer that might be able slowly leak into cells. Does unmodified dimethylpiperazine meet this criterion when buffering at pH 8? O Yes No What about buffering at pH 4? D Yes No

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The amino acid shown below has an ionizable side chain with a pka of 4. When this amino acid is in a more basic solution (i.e., pH 11), it would resemble ionization state с and have a charge of -1 dla dy HO NH₂ HO OH NH3+ OH