plz solve both I'll upvote In this peptide the amino terminus is the aminoacidCys-Ala-Gly-Arg-Gln-Meta.argb.Сysc.glnd.mete.None of these.The peptide bond *A. is formed by elimination of water betweentwo amino groups in an amino acidB. limits the possible orientations of the peptidebackbone in a proteinC. has acidic and basic characteristicsD. all these

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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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a. The graph to the right displays the degree of helicity that was measured for a peptide as nine additional amino acids were sequentially added to the initial amino acid. Describe the reasons that the helicity curve takes the shape that it does as amino acids are added on to the small peptide.
you have isolated a new protein called STICKY. you can predict from comparisons with other known proteins that STICKY contains bHLH domain. Predict the function of STICKY and rationale forthe importnce of these domains in sticky function.
The three-dimensional conformation of a protein may be strongly influenced by amino acid residues that are very far apart in sequence. This relationship is in contrast to secondary structure, where the amino acid residues are: a. always side by side. b. generally near each other in sequence. c. invariably restricted to about 7 of the 20 standard amino acids. d. often on different polypeptide strands. e. usually near the polypeptide chain's amino terminus or carboxyl terminus.
A new amino acid is found with the alpha N and backbone COOH pKa's the same as histidine but with a neutral side chain. What is the isoelectric point of this new amino acid?
Which of the following statements are correct about the native state of a protein (select all that apply)? A. Polar sidechains commonly interact with water B. Hydrophobic amino acids tend to be on surface of protein C. The sidechains of polar amino acids are most commonly found in the central core of a protein D. Formation of an alpha-helix is primarily driven by hydrogen bonds between the protein main chain, not sidechains. E. Secondary structure is largely driven by hydrophobic interactions
Which of the following peptides is more likely to take up an α-helical structure, and why?(a) LKAENDEAARAMSEA(b) CRAGGFPWDQPGTSN
Draw the ff. peptides: DK YES CHEM What is the pI of each peptide? Predict the ionic form of the peptide (given above) that will predominate at: pH 1 pH 7 pH 13
What would be the molecular sequence of the amino acid chain asp-leu-leu? (i.e. draw the whole sequence out as molecules joined together)
How do I determine an amino acid sequence from RNA? I know you start at AUG which is methionine which is an amino acid protein on the list. Not really sure how they get this when looking at the chart for amino acids. What would the full amino acid sequence for AUG CCC GUA UAA?
Draw out the peptide DPGS as it would appear in a Type II β-turn and clearly label/identify all the Hydrogen bonds present between atoms (as well as other characteristic features of the β-turn). Be sure to draw out the entire peptide and label the N- and C-termini. Which residues in this peptide are characteristic of this secondary structure and what do they do?
Which of these peptides is the most hydrophobic? A. KFYV B. ERSC C. PIMF
Amino acids project from each polypeptide backbone in a β-sheet in an alternating fashion (oneabove the plane and the next below the plane – see Fig 3.8B). Consider the following proteinsequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu.a. Is there a pattern to these amino acids? If so, what is it? b. What does this sequence of amino acids mean for the hydrophobicity/hydrophilicity of theresulting β-sheet? c. Can you make a prediction about how the β-sheet will be arranged in higher levels of protein structure? If so, what prediction would you make?

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In this peptide the amino terminus is the amino Cys-Ala-Gly-Arg-Gln-Met acid a.arg b.Cys