1) Which of the following amino acids has the highest pKa? Lys Asp Ala Trp 2)...
1) Which of the following amino acids has the highest pKa?
Lys
Asp
Ala
Trp
2) Which answer best describes the levels(s) of structure associated with a protein with two subunits in its active state?
primary
secondary
quarternary
tertiary
would have all of these levels
Homework Answers
Ans 1 : Lys
Amino acids serve as the building blocks of the protein molecules in our body. Protein performs several vital functions in our body and hence amino acids are really important to us.
Lys stands for Lysine and it has the highest pka value amongst the other amino acids mentioned. It has a pka value of 10.5 and its isoelectronic pH (pI) is 9.74.
Add Answer to:
1) Which of the following amino acids has the highest pKa?
Lys
Asp
Ala
Trp
2)...
10. The peptide shown has the amino acid sequence: A. Val-Ser-Ile-Glu-Lys B. Lys-Glu-Ile-Ser-Val C. Thr-Asp-Leu-Gln-Arg D....
10. The peptide shown has the amino acid sequence: A. Val-Ser-Ile-Glu-Lys B. Lys-Glu-Ile-Ser-Val C. Thr-Asp-Leu-Gln-Arg D. Val-Asp-Ile-Glu-Arg 11. Which of the following describes the entire three- dimensional structure of a single polypeptide? A. Secondary structure B. Quaternary structure C. Tertiary structure D. Primary structure 12. What is the primary driving force in the formation of protein tertiary structure? A. Energy released when additional ion pairs are formed. B. The exclusion of non-polar substances from aqueous solution. C. The formation of...
What fragments will be obtained by a trypsin hydrolysis of the following octapeptide? Ala-Val-Trp-Lys-Phe-Gly-Arg-Met A) Ala-Val-Trp-Lys-Phe...
What fragments will be obtained by a trypsin hydrolysis of the following octapeptide? Ala-Val-Trp-Lys-Phe-Gly-Arg-Met A) Ala-Val-Trp-Lys-Phe and Gly-Arg-Met 3) Ala-Val-Trp-Lys-Phe-Gly and Arg-Met - Ala-Val-Trp-Lys and Phe-Gly-Arg and Met ) Ala-Val-Trp-Lys and Phe and Gly-Arg and Met ) Ala-Val-Trp and Lys-Phe-Gly and Arg-Met Bradykinin is a nonapeptide, Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg. In addition to one mole of Arg, what peptides are present after hydrolysis of bradykinin with chymotrypsin? A) Arg-Pro-Pro and Gly-Phe and Ser-Pro-Phe B) Pro-Pro-Gly and Phe-Ser-Pro-Phe-Arg C) Arg-Pro-Pro-Gly-Phe and Ser-Pro-Phe ?) Arg-Pro-Pro-Gly-Phe-Ser...
3. A protein contains the following amino acids: O ALA 4 GLN 1 LEU 3 ARG...
3. A protein contains the following amino acids: O ALA 4 GLN 1 LEU 3 ARG 4 GLU 4 LYS 4 ASN 5 GLY O MET 1 ASP 1 HIS 2 PHE 4 ILE 4 PRO 8 SER 5 THR 1 TRP 2 TYR 2 VAL BGYS. a) What is its net charge at pH 1? b) What is its net charge at PH 13? c) Calculate the pl. 4. In what order would the amino acids GLU, LYS, and...
what is the prediction of the unknown amino acids mixture based on the strip from thin layer chromatography sheet? The unknown mixtures can be ala plus asp, ala plus asp plus lys, lys plus asp or ala...
what is the prediction of the unknown amino acids mixture
based on the strip from thin layer chromatography sheet?
The unknown mixtures can be ala plus asp, ala plus asp plus
lys, lys plus asp or ala plus lys.
anion exchange resin was used
Tubes 2,3, 6 and 7 had a spot appear that was light pink
We were unable to transcribe this imageWe were unable to transcribe this imageH-) to the column followed by a sufficient amount of the...
Which of these protein sequences is most likely to span a cell membrane? Gly-Asp-Val-Ala-Gly-Arg-Gly-Asn-Gly-Lys-Lys-Pro-Ser-Ser-Val-Arg-Ala-Leu-Ser Ile-Val-Leu-Pro-Ile-Val-Leu-Leu-Val-Phe-Leu-Cys-Leu-Gly-Val-Phe-Leu-Leu-Trp Lys-Asn-Trp-Arg-Leu-Lys-Asn-I
Which of these protein sequences is most likely to span a cell
membrane?
Gly-Asp-Val-Ala-Gly-Arg-Gly-Asn-Gly-Lys-Lys-Pro-Ser-Ser-Val-Arg-Ala-Leu-Ser Ile-Val-Leu-Pro-Ile-Val-Leu-Leu-Val-Phe-Leu-Cys-Leu-Gly-Val-Phe-Leu-Leu-Trp Lys-Asn-Trp-Arg-Leu-Lys-Asn-Ile-Asn-ser-Ile-Asn-Phe-Asp-Asn-Pro-Val-Tyr-Gln A. 773 B. 792 C. 811
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...
Identify the structure of amino acids, and describe the process by which they join together to...
Identify the structure of amino acids, and describe the process by which they join together to form polypeptides. Describe the 4 different groups of amino acids and their properties (Neutral, Polar, Acidic, Basic). Describe the levels of structure of proteins (primary, secondary, tertiary, and quaternary), including what bonds and interactions occur at EACH level. Describe denaturation of a protein and indicate how temperature and pH affect the protein functions. Describe the major functions of proteins
Be sure to answer all parts. An octapeptide contains the following amino acids: Ala, Pro, Gly,...
Be sure to answer all parts. An octapeptide contains the following amino acids: Ala, Pro, Gly, Asp, Trp, Lys, Leu, Met. Carboxypeptidase treatment of the octapeptide forms Asp and a heptapeptide. Treatment of the octapeptide with Chymotrypsin forms forms two tetrapeptides, A and B. Treatment of A with Trypsin yields two dipeptides, C and D. Edman degradation cleaves the following amino acids from each peptide: Gly (octapeptide),Gly (A),Met (B), Gly (C), Leu(D).Partial hydrolysis of tetrapeptide B forms Met-Pro in addition...
Review| Constants| Periodic Table Protein structure is conceptually divided into four levels, from most basic to...
Review| Constants| Periodic Table Protein structure is conceptually divided into four levels, from most basic to higher order Primary structure describes the order of amino acids in the peptide chain. Secondary structure describes the basic three-dimensional structures, a-helices and B sheets. Tertiary structure describes how the secondary structures come together to form an individual globular protein. Quatemary structure results from individual proteins coming together to form multi-subunit protein complexes Part A Complete the following vocabulary exercise relating to the level...
1. The C-terminal amino acid of the hexapeptide, Asp-Ala-ser-Glu-Val-Arg is; 2. Which of the following would...
1. The C-terminal amino acid of the hexapeptide, Asp-Ala-ser-Glu-Val-Arg is; 2. Which of the following would be observed in a person after one week of starvation? A. The brain uses glucose and ketone bodies B. Liver glycogen stores are only partially depleted due to an increase in gluconeogenesis C. Fatty acids from adipose stores are the major source of energy for red blood cells D. Muscle glycogen stores are used to maintain glucose E. Nitrogen balance is maintained because muscle...
10. The peptide shown has the amino acid sequence: A. Val-Ser-Ile-Glu-Lys B. Lys-Glu-Ile-Ser-Val C. Thr-Asp-Leu-Gln-Arg D. Val-Asp-Ile-Glu-Arg 11. Which of the following describes the entire three- dimensional structure of a single polypeptide? A. Secondary structure B. Quaternary structure C. Tertiary structure D. Primary structure 12. What is the primary driving force in the formation of protein tertiary structure? A. Energy released when additional ion pairs are formed. B. The exclusion of non-polar substances from aqueous solution. C. The formation of...
What fragments will be obtained by a trypsin hydrolysis of the following octapeptide? Ala-Val-Trp-Lys-Phe-Gly-Arg-Met A) Ala-Val-Trp-Lys-Phe and Gly-Arg-Met 3) Ala-Val-Trp-Lys-Phe-Gly and Arg-Met - Ala-Val-Trp-Lys and Phe-Gly-Arg and Met ) Ala-Val-Trp-Lys and Phe and Gly-Arg and Met ) Ala-Val-Trp and Lys-Phe-Gly and Arg-Met Bradykinin is a nonapeptide, Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg. In addition to one mole of Arg, what peptides are present after hydrolysis of bradykinin with chymotrypsin? A) Arg-Pro-Pro and Gly-Phe and Ser-Pro-Phe B) Pro-Pro-Gly and Phe-Ser-Pro-Phe-Arg C) Arg-Pro-Pro-Gly-Phe and Ser-Pro-Phe ?) Arg-Pro-Pro-Gly-Phe-Ser...
3. A protein contains the following amino acids: O ALA 4 GLN 1 LEU 3 ARG 4 GLU 4 LYS 4 ASN 5 GLY O MET 1 ASP 1 HIS 2 PHE 4 ILE 4 PRO 8 SER 5 THR 1 TRP 2 TYR 2 VAL BGYS. a) What is its net charge at pH 1? b) What is its net charge at PH 13? c) Calculate the pl. 4. In what order would the amino acids GLU, LYS, and...
what is the prediction of the unknown amino acids mixture
based on the strip from thin layer chromatography sheet?
The unknown mixtures can be ala plus asp, ala plus asp plus
lys, lys plus asp or ala plus lys.
anion exchange resin was used
Tubes 2,3, 6 and 7 had a spot appear that was light pink
We were unable to transcribe this imageWe were unable to transcribe this imageH-) to the column followed by a sufficient amount of the...
Which of these protein sequences is most likely to span a cell
membrane?
Gly-Asp-Val-Ala-Gly-Arg-Gly-Asn-Gly-Lys-Lys-Pro-Ser-Ser-Val-Arg-Ala-Leu-Ser Ile-Val-Leu-Pro-Ile-Val-Leu-Leu-Val-Phe-Leu-Cys-Leu-Gly-Val-Phe-Leu-Leu-Trp Lys-Asn-Trp-Arg-Leu-Lys-Asn-Ile-Asn-ser-Ile-Asn-Phe-Asp-Asn-Pro-Val-Tyr-Gln A. 773 B. 792 C. 811
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...
Be sure to answer all parts. An octapeptide contains the following amino acids: Ala, Pro, Gly, Asp, Trp, Lys, Leu, Met. Carboxypeptidase treatment of the octapeptide forms Asp and a heptapeptide. Treatment of the octapeptide with Chymotrypsin forms forms two tetrapeptides, A and B. Treatment of A with Trypsin yields two dipeptides, C and D. Edman degradation cleaves the following amino acids from each peptide: Gly (octapeptide),Gly (A),Met (B), Gly (C), Leu(D).Partial hydrolysis of tetrapeptide B forms Met-Pro in addition...
Review| Constants| Periodic Table Protein structure is conceptually divided into four levels, from most basic to higher order Primary structure describes the order of amino acids in the peptide chain. Secondary structure describes the basic three-dimensional structures, a-helices and B sheets. Tertiary structure describes how the secondary structures come together to form an individual globular protein. Quatemary structure results from individual proteins coming together to form multi-subunit protein complexes Part A Complete the following vocabulary exercise relating to the level...
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