A D amino acid would interrupt an alpha-helix made of L-amino acids. Another naturally occurring hindrance to the formation of an alpha-helix is the presence of:
a. a nonpolar residue near the carboxyl terminus
b. a negatively charged Arg residue
c. a positively charged Lys residue
d. two Ala residues side by side
e. a Pro residue
Can someone please explain why the answer is E.
Solution: Option E
The stability of secondary structure of protein is due to the presence of hydrogen bonding. The hydrogen bonding stablizes the alpha helices in secondary structure. Simple amino acids (like alanine) are favourable for the formation of alpha helices by hydrogen bonds between peptides.
Proline is a cyclic amino acid, therefore it is not able to form hydrogen bonds with peptides hence, tends to disrupts the alpha helices. Thus, the presence of pro-residue into the interior of proteins destablises the alpha-helix.
A D amino acid would interrupt an alpha-helix made of L-amino acids. Another naturally occurring hindrance...
A small generic section of the primary structure of an alpha helix is given below -amino acid1-amino acid2-amino acid3-amino acid4-amino acid5-amino acid-6-amino acid7- a.) which amino acid residue's backbone forms a hydrogen bond witht he backbone of the seventh(7th) residue? 6, 1, 3, 2, 5, OR 7? b.) which of the following peptide segments is most likely to be part of a stable alpha helix at physiological pH? a.) -Lys-Lys-Ala-Arg-Ser- b.) -Gly-Arg-Lys-His-Gly- c.) -Pro-Leu-Thr-Pro-Trp- d.) -Gly-Gly-Gly-Ala-Gly- e.) -Glu-Glu-Glu-Glu-Glu- f.) -Glu-Leu-Ala-Lys-Phe-...
6. The following polypeptide (30 amino acids) contains a great deal of regular secondary structure. (10) (15) (20) lys Lys Ala-Phe-Trp-Met-His- GIh-Thr-lle-Arg-Ser-Gly-Ala-Gly-Ser-Gly-Ala-Trp-Tyr-Pro-Val-Ala (30) Phe-Met-Leu-Val-Pro-Glu-Glu There are at least two regions where alpha helical structure is found. Indicate the beginning and ending residues of these regions. Any group or groups which break the alpha helical structure should not be considered part of the helix. Remember that it take four residues to give a turn of an alpha helix, so that is...
2. what is the configuration of almost all naturally occurring amino acids at the a (alpha) carbon 3. why is an alpha amino acid such as alanine more acidic than a regular carboxyllic acid 4. strecker synthesis Formation dl-phenylalanine 5. outline the steps to synthesize the simple dipeptide AL (think about two amino acids that begin with an A and an L) 6. give the structure and name of the nucleosides in dna and rna 7. give the structure of...
11.Which of the following mutations would most likely to disrupt the structure of an α-helix? Cys to Ala Lys to Arg Glu to Gly Val to Leu 12.Which amino acid combination is the most preferred to occupy positions 1 and 4 in an α-helix? Glu and Lys Phe and Pro Lys and Arg Asp and Glu 13.If each turn in the standard alpha helix extends 5.4 A and there are 3.6 amino acid residues per turn, how many amino acids...
Question 11. Certain amino acids destabilize or prevent formation of alpha-helices. Which amino acid is more likely to be found in these structures based on its charge and R-group size? A. Glycine B. Proline C. A sequence of several Glutamate D. A sequence of several Lysine E. Alanine Question 12. Which of the following is least likely to result in protein denaturation? A) Altering net charge by changing pH B) Changing the salt concentration C) Disruption of weak interactions by...
1. The following amino acid sequence is observed in an alpha-helical segment of a polypeptide: L D E N I K R N A Q L V E Q Q I R What pattern, if any, seems to characterize this sequence? Explain why this pattern might be occurring in terms of the 3D structure of the protein. 2. Indicate the probable location of the following amino acid residues in a native globular protein. a) Asp b) Phe c) Met d)...
C,D, and E i need help with.
17. The following peptide forms part of Human Hemoglobin subunit gammaa Asp-Leu-Lys-Gly-Thr-Phe-Ala A) Which amino acids are likely to be on the side of peptid acids are likely to be on the side of peptide that faces the interior of the protein? Insert your answer leu, Gto.Pne, Ala B) Which are likely to be facing the aqueous environment? Insert your answer Asp, lys, Thr Draw the structure of the sequence at pH7.4. Using...
11 Department of Biological Sciences BIOCHEMISTRY Test 2.2018 H. Nucleic Acid, Sequencing of DNA: Amino Acids Hydrolysis of salt Laboratory buffers, Polyprotie acids QUESTIONS 1. The DNA strand complementary to the strand 3-GTAGCGTAT-Y' would have the sequence a SLTACOCATAT-3 b.3.CATOXICATA-S c. 3-ATGCGTATA-S" ATATGCGTAS 2. When cytosine is treated with bisulfite, the amino group is replaced with a carbonyl group. Identify the resulting base a. adenine b. guanine c uracil d. thyminee. typoxanthine 3. How many amino acids would be in...
29. Which of the following would be synthesized in and processed by the smooth endoplasmic reticulum and Golgi apparatus? A. lipids and steroids B. DNA polymerase and RNA polymerase C. lysosomal enzymes D. cytoskeletal proteins 30. Which of the following are processed in the Golgi apparatus? A. integral membrane proteins of the plasma membrane B. proteins that are secreted from the cell C. proteins that will be broken down by lysosomes D. all of the above E. none of the...
Cyw Ala Ατα Ile Ausn Lou Asp aly Lys Ser Which molecule below is asubunit of peptide chains a. Acetic acid b. Alanine O. ATP d. Gracil Report the charge on most aqueous aspartie acid molecules at pH-7. Report the approximate p values for the amino acid whose titration curve is shown below (note there may be more slots for answer than answers). A) Value 1 B) Value 2 c) Value 3 c) Value 4 The structure of a rare...