Please explain in detail how to determine the answer : If a part of a protein...
Please explain in detail how to determine the answer :
If a part of a protein has sequence of GLEDKSA and forms one continuous α-helix, which amino acid is the carbonyl of glycine non-covalently boned to?
Homework Answers
Answer:
Amino group of K(lysine) is bonded to carbonyl of glycine by hydrogen bond.
In the alpha helix the N-H group of an amino acid forms a hydrogen bond with the C=O group of the amino acid four residues earlier. This is the most prominent characteristic of an α-helix.
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Please explain in detail how to determine the answer :
If a part of a protein...
Determine whether the sentences are true or false 27-( ) The only acidic amino acid is...
Determine whether the sentences are true or false 27-( ) The only acidic amino acid is aspartic acid. 36-( ) The quaternary structure is physically very strong because many polypeptides are clustered together. 37-( ) The amino acid sequence consisting of I-V-V-F-V is judged to form a β strand. 38-( ) The amino acid sequence consisting of A-E-A-E-L-A-L-E is judged to form an α-helix. 39-( ) If the molecular weight of glycine is 75, the molecular weight of the peptide...
please answer all parts 25) A few points: Explain how a single nucleotide substitution in the...
please answer all parts
25) A few points: Explain how a single nucleotide substitution in the sequence of a gene can: A) cause a mutation (a single amino acid replacement) in the protein coded by the gene and B) how such a single nucleotide substitution does not necessarily lead to a mutation in the protein (a silent mutation). Be very specific and use real examples for the nucletotides and the resulting amino acid in the protein. You must provide the...
A protein with the sequence below forms an alpha-helix. How many turns are made in the...
A protein with the sequence below forms an alpha-helix. How many turns are made in the helix? Explain why the properties of the amino acids in this helix result in an amphipathic protein. How might this amphipathic alpha-helix associate with the membrane? Leu-Lys-Arg-Ile-Val-Asp-Thr-Ile-Leu-Ser-Arg-Leu-Phe-Lys
please answers fast and in detail. thank youuuuu it is biochemistry question not the chemistry. By...
please answers fast and in detail. thank youuuuu
it is biochemistry question not the chemistry. By
mistake I put chemistry. please do it and send me answer as soon as
possible, thank youuuu.
Question #4 (10 points)-Mass spectroscopy Amino Acid Molecular Weight 89 174 133 146 75 146 115 137, 194 Alanine Arginine Aspartic acid Glutamic acid Glycine Lysine Proline Serine Tyrosine Valine 425, 1051 384 340 619 146 105 891 473 5301 2701 181 117 Mass/charge (here the charge...
please answer 4. Secondary structure (a-helix): The image below is of a polypeptide in secondary (2)...
please answer
4. Secondary structure (a-helix): The image below is of a polypeptide in secondary (2) structure level of protein folding. Specifically it is of an a-helix. Use the image on the left to answer the questions a-e below. The image on the right is to help with question "f' only. a. Name the specific bond/interaction indicated by the dotted lines. b. Is this bond/interaction covalent or non-covalent? c. Is this bond/interaction permanent or transient? d. What parts of the...
Protein Structure A protein contains a string of amino acids (usually more than 50) that has...
Protein Structure A protein contains a string of amino acids (usually more than 50) that has a biological function. 15ecause proteins are so large, their structure has several levels, all of which are important for the proper functioning of the protein. Ultimately, the sequence of amino acids (ordering of polar and nonpolar amino acids) dictates the 3-dimensional shape of a protein and this dictates its primary function. Level 1: Primary (1") The amino acid sequence of a polypeptide Protein Backbone...
Explain how/why the amino acid glycine and proline significantly impact the evolution of protein structure and...
Explain how/why the amino acid glycine and proline significantly impact the evolution of protein structure and function.
please answer 5. Secondary structure (B-sheet): The image below is of a polypeptide in secondary (2)...
please answer
5. Secondary structure (B-sheet): The image below is of a polypeptide in secondary (2) structure level of protein folding. Specifically it is of a B-sheet. The image on the left is of an anti-parallel sheet, and the right of a parallel sheet. a. Name the specific bond/interaction indicated by the dotted lines. b. Is this bond/interaction covalent or non-covalent? c. Is this bond/interaction permanent or transient? d. What parts of the amino acid (backbone or side chain) are...
pls try expaling this concept in as much detail as possible . this is all the informetion i eqs given to anserw the question myself Hydropathy plots are a measure of the hydrophobicity of a pr...
pls
try expaling this concept in as much detail as possible .
this is all the informetion i eqs given to anserw the question
myself
Hydropathy plots are a measure of the hydrophobicity of a protein. The free energy for transferring an amino acid in a protein from the membrane to water is plotted as a function of the position of the helix in the sequence in the protein. Numbers greeter than +84 kJ/mol on a hydropathy plot are indicative...
5. Which of the following molecules form complex structures linked by covalent bonds through Lys, HyLys,...
5. Which of the following molecules form complex structures linked by covalent bonds through Lys, HyLys, or His residues? A) Collagen B) Alpha keratin C) Hemoglobin D) Myoglobin E) Beta barrels 6. Which of the following correlates to the classic experiment demonstrating that reduced and denatured RNase A could refold into the native form? A) Disulfide bonds do not stabilize folded proteins B) Reducing agents denature proteins C) 1° structure can determine 3° structure D) Urea cleaves disulfide bonds E)...
please answer all parts
25) A few points: Explain how a single nucleotide substitution in the sequence of a gene can: A) cause a mutation (a single amino acid replacement) in the protein coded by the gene and B) how such a single nucleotide substitution does not necessarily lead to a mutation in the protein (a silent mutation). Be very specific and use real examples for the nucletotides and the resulting amino acid in the protein. You must provide the...
please answers fast and in detail. thank youuuuu
it is biochemistry question not the chemistry. By
mistake I put chemistry. please do it and send me answer as soon as
possible, thank youuuu.
Question #4 (10 points)-Mass spectroscopy Amino Acid Molecular Weight 89 174 133 146 75 146 115 137, 194 Alanine Arginine Aspartic acid Glutamic acid Glycine Lysine Proline Serine Tyrosine Valine 425, 1051 384 340 619 146 105 891 473 5301 2701 181 117 Mass/charge (here the charge...
please answer
4. Secondary structure (a-helix): The image below is of a polypeptide in secondary (2) structure level of protein folding. Specifically it is of an a-helix. Use the image on the left to answer the questions a-e below. The image on the right is to help with question "f' only. a. Name the specific bond/interaction indicated by the dotted lines. b. Is this bond/interaction covalent or non-covalent? c. Is this bond/interaction permanent or transient? d. What parts of the...
Protein Structure A protein contains a string of amino acids (usually more than 50) that has a biological function. 15ecause proteins are so large, their structure has several levels, all of which are important for the proper functioning of the protein. Ultimately, the sequence of amino acids (ordering of polar and nonpolar amino acids) dictates the 3-dimensional shape of a protein and this dictates its primary function. Level 1: Primary (1") The amino acid sequence of a polypeptide Protein Backbone...
please answer
5. Secondary structure (B-sheet): The image below is of a polypeptide in secondary (2) structure level of protein folding. Specifically it is of a B-sheet. The image on the left is of an anti-parallel sheet, and the right of a parallel sheet. a. Name the specific bond/interaction indicated by the dotted lines. b. Is this bond/interaction covalent or non-covalent? c. Is this bond/interaction permanent or transient? d. What parts of the amino acid (backbone or side chain) are...
pls
try expaling this concept in as much detail as possible .
this is all the informetion i eqs given to anserw the question
myself
Hydropathy plots are a measure of the hydrophobicity of a protein. The free energy for transferring an amino acid in a protein from the membrane to water is plotted as a function of the position of the helix in the sequence in the protein. Numbers greeter than +84 kJ/mol on a hydropathy plot are indicative...
5. Which of the following molecules form complex structures linked by covalent bonds through Lys, HyLys, or His residues? A) Collagen B) Alpha keratin C) Hemoglobin D) Myoglobin E) Beta barrels 6. Which of the following correlates to the classic experiment demonstrating that reduced and denatured RNase A could refold into the native form? A) Disulfide bonds do not stabilize folded proteins B) Reducing agents denature proteins C) 1° structure can determine 3° structure D) Urea cleaves disulfide bonds E)...
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