4. Which amino acid repeat pattern would most likely form a stable a-helix with one hydrophobicside? Explain your choiceA) (GPA).B) (ACTVMNQ)c) (DELSSHK).

Amino Acids are biochemical molecules that combine to make proteins; as a result, they are referred…

Answered: Which amino acid repeat pattern would…

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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Now consider the same protein after a post-translational modification: a kinase (enzyme) has added a phosphate to the alcohol. (Assume there no other changes in the conformation of the protein.) pka ?? 11 `NH3 `NH2 + H What is the consequence to the ratio of the amine conjugate base to conjugate acid? (The pH has not changed at this point). There will be more conjugate base because it makes a favorable hydrogen bond to the phosphate. The ratio will not change, the pKa is a constant property of any dissociable functional group. There will be less conjugate acid because it has an unfavorable ion pair with the phosphate. There will be more conjugate acid because it has an favorable ion pair with the phosphate.
determine the structure of p2 spike. is it primary, secondary, tertiary, or quaternary?
Using the letter “R" to indicate amino acid side chain, draw the following: A. The backbone atoms and bonds of a parallel ß-sheet with two B-strands of 5 amino acid each (use slide 23 of Chapter 6 for guidance). B. The backbone atoms and bonds of an antiparallel B-sheet with two B-strands of 5 amino acid each (use slide 23 of Chapter 6 for guidance). C. Draw the hydrogen bonds connecting the two B-strands in each B-sheet.
Describe/explain the role of 1-stearoyl-2-linolenyl-phosphatidylcholine in animal cells/organs
The sequence of two beta strands are shown below: Beta Strand 1: Ala-His-Thr-Tyr-Met Beta Strand 2: Gly-Cys-Asn-Gln-Lys If ONE of the H-bonding interactions that occurred was between the N-H of Gin and the C=O of Thr, what type of secondary structure element has most likely formed? Oa. Mixed beta sheet O b. Anti-parallel beta sheet O c. Parallel beta sheet O d. Alpha helix Oe. All of the above
The activity provides you with a version of the NGF pathway, an example of a RTK. All of the proteins involved can be in ON/OFF states. Using this cell signaling pathway you will be asked a variety of questions to determine how the molecules are regulated, but also how a cell would respond if this cell signaling party steps were interrupted or activated. Neural Growth Factir (NGF) Ras- Ras- GDP GTP Trk-A Ras-GEF braf braf МЕК МЕК ERK ERK ERK ERK STAT STAT Spiouty DNA Nucleus Cytosol
a) Where is the N-terminus of this peptide? Left Middle Right b) What type of secondary structure is the majority of this structure? loops alpha helix Beta sheet unstructured c) The X's indicate the alpha carbons of residues 10, 13, and 17 (labeled in the sequence above). Where would you expect this part of the structure to be found in the tertiary structure of the protein? Briefly explain your reasoning. d) The dashed line in black is indicating an interaction that is present within this structure. Draw this interaction, including all the atoms necessary for this interaction to occur. Label any partial charges present in your drawing. please upload the drawing.
4) For various amino acid pairs (for example: F to A, E to R, D to N, V to L, S to W), ask yourself: a) Based on what you know about the chemical properties of the side chains, what effect would you expect on the stability of the protein if you mutated one residue of the pair into the other in the interior of the protein? What forces might have an impact on this change (ie: what types of interactions would you expect that amino acid to be involved in?) How would your answer change if the amino acid were located on the surface of the protein? b) c)
Name the protein structural element shown in yellow in the figure: B-barrel reverse turn disordered region a-helix parallel ß sheet
6) Proteins can be modified by phosphorylation, which adds a phosphate group to the hydroxyl group of serine, threonine, or tyrosine residues. The R-group for phosphoserine is shown at right. A) The image below is an Isoelectric focusing strip that shows the unphosphorylated protein-of-interest (in blue). To which side of the unphosphorylated protein would you expect to see the phosphorylated protein? (Draw an arrow to indicate direction). Briefly justify your answer. un-phosphorylatable: Low pH Justify: B) To study the effects of phosphorylation, researchers often mutate a Ser/Thr to appear as though it is always phosphorylated or never phosphorylated at a particular site. What amino acid substitution should you use to preserve similar dimensions as Ser (or Thr) but make the side chain appear to be: constitutively (always) phosphorylated: Justify: Ser or Thr → O O=P-O O I CH₂ Ser or Thr➜ Phosphoserine High pH
1. ) In one (1) sentence point out a key structural similarity and difference in each of the following pair of terms: a) Proline and cysteine b) Secondary and Tertiary proteins c) Uracil and thymine d) AMP and dAMP e) codon and anticodon
Which of the following statements are False? (i) Parallel b-sheets characteristically distribute hydrophobic side chains on both sides of the sheet, and antiparallel B-sheets are usually arranged with all their hydrophobic residues on one side of the sheet. (ii) Planarity of the peptide bond means that no rotation occurs about the N-Ca bond while rotation is allowed about the C(O)-N and Ca-C(O) bonds. (iii) Silk fibers consist of fibroin proteins consisting of alternating A and G or S residues. (iv) If an aspartic acid residue were present in the interior of a globular protein, it would most likely be deprotonated and thus negatively charged.

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Which amino acid repeat pattern would most likely form a stable a-helix with one hydrophobic side? Explain your choice 4. A) (GPA). B) (ACTVMNQ) c) (DELSSHK).