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Indicate which secondary structure or structures (a-helix, β-pleated, random coil) will the following peptide adopt in...
(2%) Indicate which secondary structure or structures (α -helix, β -pleated, random coil) will the following...
(2%) Indicate which secondary structure or structures (α -helix,
β -pleated, random coil) will the following peptide adopt in an
aqueous solution at pH 7
(2%) The unfolding of the alpha helix of a polypeptide to a
randomly coiled conformation is accompanied by a large decrease in
a property called specific rotation, a measure of
a solution’s capacity to rotate circularly polarized light.
Polyglutamate, a polypeptide made up of only L-Glu residues, has
the alpha helical
conformation at pH 3....
6. The following polypeptide (30 amino acids) contains a great deal of regular secondary structure. (10)...
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...
A small generic section of the primary structure of an α helix is given by −amino...
A small generic section of the primary structure of an α helix is given by −amino acid1−amino acid2−amino acid3−amino acid4−amino acid5−amino acid6−amino acid7− Which amino acid residue's backbone forms a hydrogen bond with the backbone of the third (3rd) residue? Which peptide segment is most likely to be part of a stable α helix at physiological pH ? −Glu−Leu−Ala−Lys−Phe− −Gly−Arg−Lys−His−Gly− −Gly−Gly−Gly−Ala−Gly− −Pro−Leu−Thr−Pro−Trp− −Lys−Lys−Ala−Arg−Ser− −Glu−Glu−Glu−Glu−Glu− −Tyr−Trp−Phe−Val−Ile−
A small generic section of the primary structure of an alpha helix is given below -amino...
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-...
PLEASE HELP OCHEM QUESTION 1. In the following protein, identify the type of bonding or interaction...
PLEASE HELP OCHEM QUESTION
1. In the following protein, identify the type of bonding or interaction that is responsible for holding the two peptide chains together at each amino acid pair, above (A) and below (B). Gly - Ala - Ser - Cys - Val - Asp - Leu - Thr - His - Ile-Tyr-Glu - Phe - Lys - Cys - Met - Asn Val - Leu -Gin-Cys - Pro-Lys - Met - Tyr - Asp -Phe-Asn-Lys - Ile...
Based on the chemical properties of the residues, which of the following sequences could form the...
Based on the chemical properties of the residues, which of the
following sequences could form the following? At least one should
be placed in each category.
Based on the chemical properties of the residues, which of the following sequences could form the following? At least one should be placed in each category Most likely an amphipathic Most likely an amphipathic B sheet a helix Most likely a turn/ loop Not amphipathic Asn-Leu-Ala-Asp-Ser-Phe-Arg-Gin-lle Lys-Ser-Thr-Asn-Glu-Gin-Asn-Ser-Arg Gin-lle-Thr-Phe-Thr-Leu-GIn-Val-Ser Lys-GIn-Asn-Glu-Pro-Arg-Ala-Asn-Glu Arg-Phe-GIn-lle-His-Val-Gin-Phe-Glu Ala-Phe-Leu-Val-lle-Trp-Phe-Val-Ala
5. Consider the following peptide: His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gin- Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr a. What are the fragments, if it is cleaved...
5. Consider the following peptide: His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gin- Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr a. What are the fragments, if it is cleaved by trypsin? b. What are the fragments, if it is cleaved by chymotrypsin? c. What are the fragments, if it is cleaved by pepsin?
Please explain. 8. What will be the overall charge of the following peptide in the following...
Please explain.
8. What will be the overall charge of the following peptide in the following pH values? (10 points) Arg Glu Glu Lys Asn Trp Met Tyr Arg Leu Lys OH Overall 7 14 4
a. Using the table below, predict the secondary structure most likely adopted by the heptapeptide "RANGEHEAL". W...
a. Using the table below, predict the secondary structure most
likely adopted by the heptapeptide "RANGEHEAL". Will it be
alpha-helical, beta-strand, or just random coil?
b. Hydrogen bonds between backbone residues stabilize
interactions between
helixes and
sheets. Knowing this and other information about hydrogen bonds,
which amino acid from the picture below will destabilize secondary
protein structure?
Conformational Preferences of the Amino Acids Preference Amino acid a-helix B-strand Reverse turn Glu 1.59 0.52 1.01 Ala 1.41 0.72 0.82...
If mutations occur at random, and changes to 1st or 2nd "letter" of a codon usually...
If mutations occur at random, and changes to 1st or 2nd "letter" of a codon usually changes the amino acid coded for, but changes to the 3rd "letter" rarely do, roughly what % of mutations should be synonymous? Second АТ G UUU Phe UCU Ser UAU Tyr UGU Cys U 0 C | Phe UCC Ser UAC Tyr UGC Cys C Leu UCA Ser UAA Stop UGA Stop UUG Leu UCG Ser UAG Stop UGG Trp G CUU Leu CCU...
(2%) Indicate which secondary structure or structures (α -helix,
β -pleated, random coil) will the following peptide adopt in an
aqueous solution at pH 7
(2%) The unfolding of the alpha helix of a polypeptide to a
randomly coiled conformation is accompanied by a large decrease in
a property called specific rotation, a measure of
a solution’s capacity to rotate circularly polarized light.
Polyglutamate, a polypeptide made up of only L-Glu residues, has
the alpha helical
conformation at pH 3....
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...
PLEASE HELP OCHEM QUESTION
1. In the following protein, identify the type of bonding or interaction that is responsible for holding the two peptide chains together at each amino acid pair, above (A) and below (B). Gly - Ala - Ser - Cys - Val - Asp - Leu - Thr - His - Ile-Tyr-Glu - Phe - Lys - Cys - Met - Asn Val - Leu -Gin-Cys - Pro-Lys - Met - Tyr - Asp -Phe-Asn-Lys - Ile...
Based on the chemical properties of the residues, which of the
following sequences could form the following? At least one should
be placed in each category.
Based on the chemical properties of the residues, which of the following sequences could form the following? At least one should be placed in each category Most likely an amphipathic Most likely an amphipathic B sheet a helix Most likely a turn/ loop Not amphipathic Asn-Leu-Ala-Asp-Ser-Phe-Arg-Gin-lle Lys-Ser-Thr-Asn-Glu-Gin-Asn-Ser-Arg Gin-lle-Thr-Phe-Thr-Leu-GIn-Val-Ser Lys-GIn-Asn-Glu-Pro-Arg-Ala-Asn-Glu Arg-Phe-GIn-lle-His-Val-Gin-Phe-Glu Ala-Phe-Leu-Val-lle-Trp-Phe-Val-Ala
5. Consider the following peptide: His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gin- Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr a. What are the fragments, if it is cleaved by trypsin? b. What are the fragments, if it is cleaved by chymotrypsin? c. What are the fragments, if it is cleaved by pepsin?
Please explain.
8. What will be the overall charge of the following peptide in the following pH values? (10 points) Arg Glu Glu Lys Asn Trp Met Tyr Arg Leu Lys OH Overall 7 14 4
a. Using the table below, predict the secondary structure most
likely adopted by the heptapeptide "RANGEHEAL". Will it be
alpha-helical, beta-strand, or just random coil?
b. Hydrogen bonds between backbone residues stabilize
interactions between
helixes and
sheets. Knowing this and other information about hydrogen bonds,
which amino acid from the picture below will destabilize secondary
protein structure?
Conformational Preferences of the Amino Acids Preference Amino acid a-helix B-strand Reverse turn Glu 1.59 0.52 1.01 Ala 1.41 0.72 0.82...
If mutations occur at random, and changes to 1st or 2nd "letter" of a codon usually changes the amino acid coded for, but changes to the 3rd "letter" rarely do, roughly what % of mutations should be synonymous? Second АТ G UUU Phe UCU Ser UAU Tyr UGU Cys U 0 C | Phe UCC Ser UAC Tyr UGC Cys C Leu UCA Ser UAA Stop UGA Stop UUG Leu UCG Ser UAG Stop UGG Trp G CUU Leu CCU...
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