Select the true statements about protein secondary structure.In an a-helix, the side chains are located on the outside of the helix.The secondary level of protein structure refers to the spatial arrangements of short segments of the protein.In a B-pleated sheet, the side chains are located between adjacent segments.Peptide bonds stabilize secondary structure.The x-helix is held together by hydrogen bonds between the amide N-H and C=O groups.Incorrect

The polypeptide chain undergoes folding in order to acquire a three dimensional conformation that is…

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Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

Give an example of a protein that has quaternary structure. How many polypeptide chains are present in this protein?
"Loops of polypeptide that protrude from the surface of a protein often form the binding sites for other molecules" is true or false.
Draw beta sheet with backbone hydrogen bonds, is this structure on the interior or exterior of the protein and why? Region 1: -Ser-Thr-Glu-His- Region 2: -Asp-Tyr-Lys-Asn
Within a naturally-occurring polypeptide, under neutral pH conditions (pH = 7.0), which of the following amino acids always has a negatively charged carboxyl group? the first amino acid in the primary structure histidine lysine arginine the last amino acid in the primary structure
The bottom peptide segment is found in the secondary structure composed of anti-parallel - sheets. From the C-terminus of the peptide below, the sequence immediately after alternation contains the following amino acid residues (from N → C) A-F-R-M-Y-A. a) which side do you expect to face the solvent? Briefly explain your reasons NH, но Nterminus
Which of the numbered bonds in this polypeptide fragment are peptide bond(s)? (Select all that apply!)
Sort the images according to the level of structure in the proteins shown. Sort the items into the appropriate bin. ▸ View Available Hint(s) Reset Help Primary structure Secondary structure Tertiary structure Quaternary structure Mis
Select the correct match : 1.Reducing sugar — Sucrose 2.Phosphodiester bond — Between nucleotides on antiparallel strands of DNA 3.Glycosidic bond — Between repeating units of starch and in glycogen 4.Peptide bond — Formed by elimination of H2 between amino acids
Your friend has discovered a protein that they suspect is glycosylated. They decide to perform a series of tests to determine the nature of the oligosaccharide. Assuming/Knowing the following: Fucose molecular weight is approximately 164 Galactose molecular weight is approximately 180 GalNAc molecular weight is approximately 221 Mannose molecular weight is approximately 180 Sialic Acid molecular weight is approximately 309 Neuraminidase cleaves before a Sialic Acid (Sialic Acid and anything after leaves the protein) Beta-galactosidase cleaves after a Galactose (Galactose and anything before remains on the protein) Peanut Agglutinin binds to GalNAc Concanavalin A binds to Mannose Hemagglutinin binds to Sialic Acid Based on preliminary results, they suspect that the oligosaccharide is 7 glycosides long and weighs a total of 1414 g/mol They carried out the following experiments: they treated the protein with either a glycosidase or a lectin, and then pelleted the protein using…
Below is the primary structure of a protein. A R 1 I I H H || O H 1 Psi bond [Select] Phi bond [Select] N-terminus [Select] B C D H O I || C-terminus [Select] NC-C-N-C-C-N-C-C-N-C-C-N-C-C - N... I 1 H H I R R H I 11 O HO I || R R I I H a. For each part of the question, select the letter associated the with appropriate component of the structure. Peptide bond [Select] I H U MO b. Which letter represents a bond without 360-degree rotation? [Select] H |
Which of the following is/are least likely to be found in an alpha helix because it has an inappropriate Phi angle. a Polar charged amino acids b Proline c Nonpolar amino acids d Glycine e Polar uncharged amino acids
What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct. the surface consists of hydrophilic alpha-helix. the surface is highly modified by post-translational modification. the surface is permanently bound by chaperones. the surface is unstructured. the surface, or part of it, is self-complementary.

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