Predict the amino acid sequence based on the conditions below. Use the one-letter abbreviation of amino acids.a. The amino acid in the C-terminal is optically inactive.b. The fifth amino acid is a neutral aromatic amino acid that yields a negative result for the Xanthoproteic test using intact protein while producing a yellow soln withXanthoproteic reagent and yielding a negative result with Hopkin's Cole test using basic hydrolysate.c. Yields serine and a hexapeptide after treatment of aminopeptidase (specificity: peptide bond on the N-terminus).d. The amino acid beside the N-terminal a.a. will yield ornithine and urea after alkaline hydrolysis.e. The third amino acid gives a positive result for Hopkins-Cole Test.f. Chymotrypsin cannot cleave the peptide bond on the fifth amino acid because of the presence of this a.a. residue.g. The amino acid at the carboxy-end of the third a.a. will yield a black precipitate for Pb(Ac)2.

Amino acids are building block of polypeptide chain. its alpha carbon contains carboxyl group, amine…

Answered: Predict the amino acid sequence based…

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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Similar questions

Sketch the appearance after visualization of a protein mixture containing the seven proteins above when subjected to two-dimensional (2D) gel electrophoresis.
Provide examples of amino acids that would yield a positive Azo Dye test and amino acids that would yield a negative Azo Dye test. Show the structures.
an protein has a molecular wieght of 90 KD when purified by gel filtration and has a molecular wieght of 60 KD hen purified by electrophoresis which one is the more selective?
Complete the table below by adding (+) or (-) if eahc sample (amino acid or protein) below will test positive or negative, respectively. sample BIURET NINHYDRIN XANTHOPROTEIC MILLON-NASSE SAKAGUCHI LEAD ACETATE PAULY HOSKIN-COLE G W H Y C R HAIR GELATIN CASEIN PEPTONE Identify the amino acid that will give the following data: BIURET NINHYDRIN XANTHOPROTEIC MILLON-NASSE SAKAGUCHI LEAD ACETATE PAULY HOPSKIN-COLE - + + + - - + - Name of amino acid: structurte of the amino acid:
Five amino acids were subjected to normal phase chromatography, and the following Rf values were computed: A - 0.59 B - 0.12 C - 0.71 D - 0.33 E - 0.20 Which is the most polar amino acid?
Upon doing the experiment of Protein Denaturation, what could happen in the precipitation of strong acids if small amount of water is added to albumin solution added to a test tube and added to another tube containing concentrated nitric acid? Explain clearly.
Upon doing the experiment of Protein Denaturation, what could be observed in the precipitation of heavy metal ions if an albumin solution in a test tube is dropped with drops of silver nitrate and then it will be shaken? Explain.
What is the Rf value of each amino acid sample? Arrange the amino acids from most non-polar to least non-polar. What is the possible identity of the unknown amino acid? Answer can be up to two amino acids.
Explain the Rf value obtained on the basis of the structure of amino acids use. Explain in 1-3 sentence only.
A mixture of amino acids that do not separate sufficiently when a single technique is used can often be separated by two-dimensional chromatography. In this technique, the mixture of amino acids is applied to a piece of filter paper and separated by chromatographic techniques. The paper is then rotated 90°, and the amino acids are further separated by electrophoresis, producing a type of chromatogram called a fingerprint. Identify the spots in the fingerprint obtained from a mixture of Ser, Glu, Leu, His, Met, and Thr.
If 1ml of an unknown sample of protein is diluted to 10ml, and a 0.5ml portion of the diluted sample is found to contain 50ug of protein when assayed for protein using the lowry method. If you mix two unknown samples and repeat the lowry assay, is the absorbance equivalent to the sum of the two individual unknown samples that is used?
Consider the following properties of the protein components of a sample mixture as provided in the table below: 1. if the mixture is subjected to gel filtration chromotography which protein component elute first? 2. if the mixture is subjected to isoelectric focusing which protein will stop m oving nearest to the positive electrode? 3. if the mixture is subjected to cation-exchange chromotography using a buffer at ph 7 which protein will bind to the resin? 4.if the mixture is subjected to SDS-PAGE which protein will be at bottomost portion of gel? 5.if the mixture is subjected to hydrophobic interaction chromotography which protein will bind most strongly to the resin?

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