Can anyone please draw examples of the structures formed in the myristoylation and palmitoylation of a protein with the...
Can anyone please draw examples of the structures formed in the myristoylation and palmitoylation of a protein with the shown correct chemical linkage to the protein and the amino acids involved.
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Can anyone please draw examples of the structures formed in the myristoylation and palmitoylation of a protein with the...
The primary structure of a protein is formed by the condensation of amino acids in a...
The primary structure of a protein is formed by the condensation of amino acids in a certain sequence. Consider the dipeptide formed by the condensation of glycine and tyrosine in Figure 8.31B. a. Draw the structure of the dipeptide that would be formed if the two amino acids condensed in the opposite sequence. b. How are the structures of the dipeptides in Figure 8.31B and your drawing related to each other? B 0 HN-C-0--OH HO H-N-C-C-OH H CHE H OH...
QUESTION 2 Select the CORRECT statements (chose all that are correct). Secondary protein structures are held...
QUESTION 2 Select the CORRECT statements (chose all that are correct). Secondary protein structures are held together by disulphide bridges/bonds. Alpha helices and beta sheets are common secondary protein structures. Tertiary protein structures are held together by covalent bonds only. Secondary protein structures are held together by hydrogen bonds only. All proteins have a quaternary protein structure. Amino acids linked with a peptide bond make up the primary protein structure.
please answer! 3) Protein structure and amino acid side chains a) Give examples of the types...
please answer!
3) Protein structure and amino acid side chains a) Give examples of the types if attractive forces found between the side chains of the following amino acid residue pairs at pH 7.4 00 Leu and Phe (ii) Two Cys (ii) Asp and Thr (iv) Asp and Arg b) Of the 4 levels of protein structure, which ones are stabilized by interactions between amino acid side chains? c) Identify the two regular types of secondary structures and describe the...
B. DIPEPTIDES Draw the two dipeptides which can be formed from serine and cysteine. Circle the...
B. DIPEPTIDES Draw the two dipeptides which can be formed from serine and cysteine. Circle the amide bonds. Hint: It helps to draw the amino group to the left and carboxyl to the right when orienting the amino acids. Ser-Cys Cys-Ser
1) Name the following molecule: 2) Draw the organic products formed in the following reactions. K.C.07...
1) Name the following molecule: 2) Draw the organic products formed in the following reactions. K.C.07 H₂SO4, H₂o 3) Rank the following organic acids according to strength with 1 being the strongest acid 41 Draw il resonance structures of the fold r Carboxylic acids often exist as dimers, where two molecules are attached to each other Propose a reason. b. Draw an example of this phenomenon between two molecules of acetic acid (CH.COOH) Answer the following questions about the amino...
please help me type my introduction for my lab report. thank you!! INTRODUCTION In this section,...
please help me type my
introduction for my lab report. thank you!!
INTRODUCTION In this section, you will introduce the experiment by explaining generally what you did and why you did it. This section usually starts with an examination of the literature through a library search to inform the reader about work already done on this topic. If you have never done a bibliographic database search for scientific journal articles, then you are not yet a biological sciences major (note:...
Explain how Niacin can be used to reduce a ketone. Please provide a mechanism. Draw by...
Explain how Niacin can be used to reduce a ketone. Please provide a mechanism. Draw by hand Explain how a cell ubiquitinates a protein and provide two possible reasonings for doing so. Explain how high levels of amino acids can act as feedback inhibitors.
Please describe the technique thoroughly and give examples of proteins that would be involved in ...
Please describe the technique thoroughly and give examples of proteins that would be involved in the analysis. Limitations/advantages? how do you differentiate or if its good for small or large amino acids? Protein Analysis: For each of the techniques, we covered you should understand the basics of what the technique can be used to discover SDS-Page/ coomassie blue Western blot (focus on the part after SDS-PAGE) Protease Digestion & Mass Spec Crystallography Edman Degradation NMR I may ask you to...
Question 1 (0.5 points) Saved Proteins are formed by joining together. carboxylic acids fatty acids amino...
Question 1 (0.5 points) Saved Proteins are formed by joining together. carboxylic acids fatty acids amino acids none of the above Question 2 (0.5 points) Which two functional groups does an amino acid contain? amine and carboxylic acid carboxylic acid and amide amide and heterocyclic ring heterocyclic ring and amine Question 3 (0.5 points) Do amino acids commonly exist in nature as neutral molecules with all uncharged atoms? Yes No Question 1 (0.5 points) What is a protein? A polymer...
Describe the chemical properties of amino acids and discuss how they can affect the final structu...
Describe the chemical properties of amino acids and discuss how they can affect the final structure of a folded protein. In your answer, give examples of amino acid substitutions that could cause changes to a protein’s structure and function
The primary structure of a protein is formed by the condensation of amino acids in a certain sequence. Consider the dipeptide formed by the condensation of glycine and tyrosine in Figure 8.31B. a. Draw the structure of the dipeptide that would be formed if the two amino acids condensed in the opposite sequence. b. How are the structures of the dipeptides in Figure 8.31B and your drawing related to each other? B 0 HN-C-0--OH HO H-N-C-C-OH H CHE H OH...
QUESTION 2 Select the CORRECT statements (chose all that are correct). Secondary protein structures are held together by disulphide bridges/bonds. Alpha helices and beta sheets are common secondary protein structures. Tertiary protein structures are held together by covalent bonds only. Secondary protein structures are held together by hydrogen bonds only. All proteins have a quaternary protein structure. Amino acids linked with a peptide bond make up the primary protein structure.
please answer!
3) Protein structure and amino acid side chains a) Give examples of the types if attractive forces found between the side chains of the following amino acid residue pairs at pH 7.4 00 Leu and Phe (ii) Two Cys (ii) Asp and Thr (iv) Asp and Arg b) Of the 4 levels of protein structure, which ones are stabilized by interactions between amino acid side chains? c) Identify the two regular types of secondary structures and describe the...
B. DIPEPTIDES Draw the two dipeptides which can be formed from serine and cysteine. Circle the amide bonds. Hint: It helps to draw the amino group to the left and carboxyl to the right when orienting the amino acids. Ser-Cys Cys-Ser
1) Name the following molecule: 2) Draw the organic products formed in the following reactions. K.C.07 H₂SO4, H₂o 3) Rank the following organic acids according to strength with 1 being the strongest acid 41 Draw il resonance structures of the fold r Carboxylic acids often exist as dimers, where two molecules are attached to each other Propose a reason. b. Draw an example of this phenomenon between two molecules of acetic acid (CH.COOH) Answer the following questions about the amino...
please help me type my
introduction for my lab report. thank you!!
INTRODUCTION In this section, you will introduce the experiment by explaining generally what you did and why you did it. This section usually starts with an examination of the literature through a library search to inform the reader about work already done on this topic. If you have never done a bibliographic database search for scientific journal articles, then you are not yet a biological sciences major (note:...
Question 1 (0.5 points) Saved Proteins are formed by joining together. carboxylic acids fatty acids amino acids none of the above Question 2 (0.5 points) Which two functional groups does an amino acid contain? amine and carboxylic acid carboxylic acid and amide amide and heterocyclic ring heterocyclic ring and amine Question 3 (0.5 points) Do amino acids commonly exist in nature as neutral molecules with all uncharged atoms? Yes No Question 1 (0.5 points) What is a protein? A polymer...
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