A protein has the amino acid sequence DSRLSKTMYSIEAPAKLDWEQNMAL How many peptide fragments would result from cleaving the sequence with each reagent. cyanogen bromide: 3 trypsin: 4 chymotrypsin: 3 Incorrect Which of these three reagents gives the smallest single fragment (in number of amino acid residues)? Otrypsin cyanogen bromide Ochymotrypsin Incorrect

A protein has the amino acid sequence DSRLSKTMYSIEAPAKLDWEQNMAL How many peptide fragments would result from cleaving the sequence with each reagent. cyanogen bromide: 3 trypsin: 4 chymotrypsin: 3 Incorrect Which of these three reagents gives the smallest single fragment (in number of amino acid residues)? Otrypsin cyanogen bromide Ochymotrypsin Incorrect

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter9: Gene Expression And Gene Regulation

Section: Chapter Questions

Problem 19QP: Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the...

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Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the N-terminus and C-terminus. Draw a box around the peptide bonds.
Residues such as valine, leucine, isoleucine, methionine, andphenylalanine are often found in the interior of proteins,whereas arginine, lysine, aspartic acid, and glutamic acid areoften found on the surface of proteins. Suggest a reason forthis observation. Where would you expect to find glutamine,glycine, and alanine?
Explain how tandem mass spectroscopy is used to determinethe sequence of a peptide. Once a peptide sequence is known,how is this information used to determine the sequence of theentire protein?
* Draw the tripeptide FTQ, making sure to care for stereochemistry.* Identify the N-terminus and the C-terminus of the peptide.* Identify what type of stabilizing interactions the amino acid side chains could employ in the tertiary andquaternary structure of a protein.
Draw the structure of the following polypeptide at physiological pH. You do not need to indicate the names or abbreviations. Also highlight the phi and psi bonds around the third amino acid. Protein sequence: PARTICLE Protein sequence: NEDSTARK
A peptide has the following amino acid composition:2 Met, 2 Phe, 2 Glu, 1 Arg, 1 Lys, 1 Val, 1 Leu, 1 Gly, 1 SerReaction of the intact peptide with Sanger’s Reagent followed by acid hydrolysis creates a derivative of Met. A specific cleavage of the intact peptide using chymotrypsin produces fragments with the following sequences:Fragment A: Glu-Gly-Lys-Phe Fragment B: Met-Ser-Leu-Arg Fragment C: Met-Val-Glu-Phe What is the polypeptide sequence? (You may use the three-letter symbol for each amino acid in the sequence).
Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on primary amino acid sequence data Consider the following amino acid sequence Ile-Ala-His-Thr-Tyr-Gly-Pro-Phe-Glu-Ala-Ala-Met-Cys-Lys-Trp-Glu-Ala-Gln-Pro-Asp-Gly-Met-Glu-Cys-Ala-Phe-His-Arg Where might reverse turns occur? Where might Intrachain disulfide linkages be formed? What will be the secondary structure formed from this sequence? Assuming that this sequence is part of a larger globular protein, indicate the probable location of the following amino acid residues: Asp, Ile, Thr, Ala. Gln, Lys.( Hint: see Hydropathy index)
Predict the protein 3° structure of the following protein sequence. Provide detail from 2° structure principles Nterm – SLDVTFSPGAEITFKWNPGSFNSLKDTIRQVTDK – Cterm
Amino acid sequence in a protein that can form N-glycosylation is called a glycosylation sequon. Which of the following is such a sequon? a. Asn-Ala-Thr b. Gln-Ala-Thr c. Asn-Pro-Pro d. Asn-Ala-Ala e. Gln-Ala-Ala
A tetradecapeptide (14 amino acid residues) gives the following peptide fragments on partial hydrolysis. From this information, deduce the primary structure of this polypep- tide. Fragments are grouped according to size. Pentapeptide Fragments Tetrapeptide Fragments Phe-Val-Asn-Gln-His Gln-His-Leu-Cys His-Leu-Cys-Gly-Ser His-Leu-Val-Glu Gly-Ser-His-Leu-Val Leu-Val-Glu-Ala
When will scientists be able totake any amino acid sequence andaccurately predict both that protein’sthree-dimensional conformationsand its chemical properties? Whatbreakthroughs will be needed toaccomplish this important goal?
The amino acid sequence of three peptide fragments are shown below. Peptide 1: QAMGRAGDLKYLGLHSV Peptide 2: ALMALFMVMALVLVSVLFIA Peptide 3: MVEDLLKQIARYLISE (a) Circle all of the charged residues in peptide 1 (assume pH =7.0). Box all of the aromatic residues in peptide 2. Underline all of the nonpolar residues in peptide 3. (b) Determine the net charge of the predominant form of each of the peptides at pH 4.5 and pH 11.5. Assume the ionizable groups have the pKa values listen in Table 2.1 of your text. (c) Which of these peptides would be most likely to be found as an alpha helix in a soluble (cytoplasmic) protein? Which would be most likely to be found as an alpha helix in a transmembrane protein? Which would be least likely to form an alpha helix of any kind?