11) Proline and glycine are sometimes known as helix breakers because they disrupt the alpha helical back bone conformation; however both have unusual conformational abilities and are commonly found in turns. Amino acid that prefer to adopt helical conformations in proteins include lysin,glutamate ,alanine etc.
12) Detergents can be denaturing or non denaturing depending upon the protein structure. So it is least likely to cause protein denaturation.
13) Alpha helices have 3.6 anino acid residues per turn.
14) Proline and glycine are found in beta turns.
15) C-C-N-C-C-N
16) Placement of hydrophobic amino acid residues with in the interior of the protein.
Question 11. Certain amino acids destabilize or prevent formation of alpha-helices. Which amino acid is more...
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...
24. The _______ of amino acids in a protein is referred to as its primary structure. A) twisting B) sequencing C) folding D) none of these 25. The structure of a protein is most important because the _______ of the amino acids determines its overall shape, function and properties. A) primary, twisting B) primary, sequencing C) secondary, twisting D) secondary, folding E) none of these 26. The secondary structure of a protein is due to_______ between amino acid residues. A) hydrophobic interactions B) hydrogen bonding...
QUESTION 9 Sequence analysis of a membrane protein shows four 20 amino acid long stretches of residues that are predominantly hydrophobic Between each of these stretches of hydrodophobic residues, a stretch of predominantly hydrophilic residues is found. From this observation one can reasonably postulate that: A this is a 4 stranded beta barrel which spans the membrane B.this is a glycoprotein o this protein has 4 alpha helical segments that span the membrane o this protein can be removed from...
Hydrophobic interactions may occur between the R-groups of which of the following pairs of amino acids: A. Arg and His B. His and Asp C. Tyr and Gly D. Phe and Trp E. Val and Asn
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)...
Understand alpha helices and beta pleated sheets Question Every helical turn in an a-helix has 3.6 amino acid residues. Then, hydrogen bonds are formed between the oxygen atom in amino acid along the the carbonyl group in the first amino acid and the hydrogen atom in the amine group of the chain. Select the correct answer below: third second fourth fifth FEEDBACK MORE INSTRUCTION SUBMIT Content attribution
A chain GIVEQCCASVCSLYQLENYCN B chain FVNQHLCGSHLVEALYLVCGERGFFYTPKA Shown above is the amino acid sequence of the hormone insulin. This structure was determined by Frederick Sanger and his coworkers. Most of this work is described in a series of articles published in the Biochemical Journal from 1945 to 1955. When Sanger and colleagues began their work in 1945, it was known that insulin was a small protein consisting of two or four polypeptide chains linked by disulfide bonds. Sanger and his coworkers...
All amino acids in proteins are Select one: O a. alpha-amino acid O b. (R)-amino acids c. acidic O d chiral
Question 5. Which of the following pairs of bonds within a peptide backbone show free rotation around both bonds? A) Ca-C and N-C B) C-O and N-C C) C-O and N-Ca D) N-C and Ca-C E) N-Ca and N-C Question 6. In the diagram below, the plane drawn behind the peptide bond indicates the: A) absence of rotation around the C-N bond because of its partial double-bond character. B) plane of rotation around the C-N bond. region of steric hindrance...
Question 5 Bio206 Homework 6 Amino Acids and Proteins Organic Chemistry II Due May 6, 2017 1. Which amino acid is least likely to be found in a natural protein? CH20H NHz CHs IV 2. A pentapeptide has the molecular formula: Asp, Glu, His, Phe, Val. Partial hydrolysis of the pentapeptide gives: Val Asp, Glu His, Phe Val, and Asp Glu. What is the amino acid sequence of the pentapeptide? 3. When the pentapeptide below is heated first with 2,4-dinitrofluorobenzene...