amino acid in the form of a "phenylthiohydantoin" (PTH-amino acid), are shown below. What is the expected outcome if the N-terminal amino acid is proline (Pro)? (The structure of proline is provided below for your reference.)

Q: Consider the following tetrapeptide, written in a sequence according to normal convention, from left…

A: The given tetrapeptide has an acidic residue at the first position, the second residue is cysteine,…

Q: What is the expected molecular weight of the protein encoded by the sequence provided here:

A: A protein is formed by various amino acids linked together by peptide bonds. By knowing the number…

Q: Consider the peptides Pro-Gin-Val-Phe-His-Asp-Cys and His-Gln-Pro-Cys-Asp-Phe-Val. How do these two…

A: Amino acids are biomolecules in which an amino group and a carboxyl group are linked to the same…

Q: how does the protein environment surrounding an amino acid chain affect its chemical…

A: The chemical properties of an amino acid within a protein are significantly influenced by its…

Q: Normal hemoglobin (HbA) leu thr glu glu lys Sickle cell hemoglobin (HbS) leu thr pro val glu lys ser…

A: Sickle cell anemia is a genetic blood disorder characterized by abnormal, crescent-shaped red blood…

Q: 6. Would Lys-Glu-Ser have the same pl as Ser-Glu-Lys? Explain.

A: Note: The given picture contains multiple questions and as per the guidelines we'll answer the first…

Q: After a polypeptide chain has been synthesized, certain amino acids in the peptide may become…

A: The modified amino acid shown in the structure you provided is serine (Ser).The modification that…

Q: Use the pka values, calculate the isoelectric point (pl) of the following amino acids. a) Leucine b)…

A:

Q: A) Draw the "standard" base pairs (A:T and G:C) but instead of using the most common form of each…

A: Hi! Thanks for your question. As you have posted multiple questions and have not mentioned which one…

Q: When answering the questions below, please use the one-letter code for the amino acid, with NO…

A: Acid hydrolysis: Acid hydrolysis of any protein/polypeptide is being used to detect amino acids…

Q: If these amino acids are separated using electrophoresis and pH = 6, will the glutamic acid move to…

A: The isoelectric point of an amino acid is the pH at which the net electric charge of that amino acid…

Q: Find the charge of the peptide KEALYR at pH 7.2. Below is the pKa chart. Provide your answer up to…

A: Before going into the intricate and precise calculation that gives us the charge of the given…

Q: Using proper convention, provide the amino acid sequence for the following peptide.

A: To provide the amino acid sequence for the given peptide, let's break down the structure into its…

Q: Draw a Lineweaver-Burke plot with two lines, one representing an uninhibited enzyme and another…

A: Competitive inhibition of Lineweaver–Burk plot increases the slope of the line and alters the…

Q: Many bioactive compounds are derived from amino acids. This compound, found in trace amounts in…

A: Amino acids are the molecules that join to form a protein structure. The bond formed between two…

Q: Identify the following non-chiral molecule:  NH2-CH2-COOH (dry form) aspartic acid arginine glycine…

A: Amino acids are small molecules made up of carbon, hydrogen, nitrogen and oxygen in some cases…

Q: What type of noncovalent interaction occurs between the glutamine and threonine side chains? Draw…

A: Non-covalent interactions are the weekly sharing of electrons between the atoms whereas it was an…

Q: On the paper provided, draw the chemical structure of a peptide with a sequence LEMD at pH 7. The…

A: Here, we are given the peptide LEMD. There are 4 ionizable groups in the peptide. They…

Q: Are phosphate groups considered negatively charged and acidic (because the negative charge is due to…

A: Amino acids are the basic unit of proteins. There can be different types of R groups in each amino…

Q: Provide the number of polypeptide chains present and the number of amino acid residues in each…

A: We need to tell how many polypeptide chains are there and how many amino acid residues are found in…

Osmosis

In simple words, osmosis is the slow, gradual movement of a liquid through a membrane. But there are nuances to this process. For instance, there has to be an imbalance in the distribution of solute in the liquid on either side of the membrane, which has to be semipermeable. The liquid in the region with a lower solute concentration moves to the region with a higher concentration, thereby displacing the solution in the process. The objective is to equalize the concentration of molecules on both sides of the membrane; the displacement of liquid can be viewed as a byproduct of this equalization. Since there is no energy required to carry osmosis, it is considered a passive process.