usIn an alpha helix,0the peptide chain is fully extendedOthere are hydrogen bonds parallel to the helix axisthere are hydrogen bonds perpendicular to the direction of the polypeptide chainO there are no hydrogen bondsQuestion 56The protein myoglobinO contains a heme groupO all of the choices are truecarries oxygen in the bloodstreamO contains a high degree of ß-pleated sheet structure LISWhich amino acid has a guanidino group?Uhistidineargininetryptophanaspartic acidQuestion 54Which amino acid has a polar, non-titratable R group?O arginineO histidineO prolineO serine

Amino acids are the building blocks of proteins . They are joined by Peptide bond to form a linear…

In an alpha helix, U the peptide chain is fully extended there are hydrogen bonds parallel to the helix axis there are hydrogen bonds perpendicular to the direction of the polypeptide chain O there are no hydrogen bonds Question 56 The protein myoglobin O contains a heme group O all of the choices are true O carries oxygen in the bloodstream O contains a high degree of B-pleated sheet structure

In an alpha helix, U the peptide chain is fully extended there are hydrogen bonds parallel to the helix axis there are hydrogen bonds perpendicular to the direction of the polypeptide chain O there are no hydrogen bonds Question 56 The protein myoglobin O contains a heme group O all of the choices are true O carries oxygen in the bloodstream O contains a high degree of B-pleated sheet structure

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter3: Biological Molecules: The Carbon Compounds Of Life

Section: Chapter Questions

Problem 9TYK: In living systems: a. proteins rarely combine with other macromolecules. b. enzymes are always...

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In living systems: a. proteins rarely combine with other macromolecules. b. enzymes are always proteins. c. proteins are composed of 24 amino acids. d. chaperonins inhibit protein movement. e. a protein domain refers to the place in the cell where proteins are synthesized and function.
At what level of protein structure (primary, secondary, tertiary, or quaternary) will protein structure be initially altered? A mutation in the genetic sequence, which ultimately causes an amino acid to change(e.g. Trp – Asn – His turns into Trp – Arg – His) Dissolving a protein in a non-polar solvent (like oil) instead of water.
Indicate the level(s) of protein structure to which each of thefollowing contributes:a. amino acid sequenceb. b-pleated sheetc. hydrogen bondd. disulfide bond
The R-group of lysine has an overall positive charge. The R-group of glutamic acid has an overall negative charge. Within the structure of a protein molecule, these two amino acids will: O attract each other O repel each other O form a disulfide bridge O form a pure covalent bond
Fill in the following with the specific bond(s): Maintain(s)the helical structure of many proteins____________: ;link(s) polypeptide chains and can cause proteins tobend:_______ and________ ; join(s) the twostrands of the double helix of DNA:_________ ; link(s) amino acids to form the primary structure of proteins:_______.
In the ER lumen nascent polypeptide chains are kept from misfolding or aggregating until an entire domain or polypeptide is completed and can fold properly. true false
Which levels of protein structure are determined by primary structure (i.e. the specific amino acid sequence beginning at the amino terminus of the polypeptide)? Mark all that apply. 1. secondary structure (alpha helices and/or beta sheets) 2. tertiary structure (the folded, three-dimensional shape of a protein) 3. amino acids 4. peptide bonds
In the alpha-helices, which of the following statement is NOT true? a. Backbone carbonyl oxygen of residue (i) hydrogen bonds to backbone NH of the fourth residue of chain of residue (i + 4). b. Side chains project out from an α-helix. c. Hydrogen bonds are almost straight and parallel to the helix axis. d. Helix has a macrodipole. e. The rise or advance per amino acid residue is 0.54 nm.
For this homework it’s a protein but I am stuck because it asks This molecule can have _____ levels of structure And then it asks What level of structure is shown in this protein marcromolecule Then asks if I add another chain to this molecule what level of structure will that be? What are the other levels of structure it can have and how are they formed
A denatured protein has lost its _______ .a. hydrogen bondsb. shapec. functiond. all of the above
Peptide bond is /has ……………. This structural feature prevents protein to sample all possible conformations available can you fill in the blanks
Please Answer numbers 1, 2 & 3 thank you 1. Which of the following intermolecular molecular forces of attraction is disrupted when a native protein is added with acetic acid? a. Hydrogen bond b. Peptide bond c. Disulfide bond d. Salt bridge e. van der Waals force 2. Suppose a protein sample with a fragment containing the following amino acid sequence is subjected to various chemical assay/tests. - Ala-Gly-Phe-Met-Cys- which of the following test will the sample be positive? a. Lead-sulfide test b. Hopkins cole's test c. Millon's test d. Xanthoproteic test 3. Suppose a protein sample with a fragment containing the following amino acid sequence is subjected to various chemical assay/tests. - Ala-Gly-Trp-Phe-Met-Cys- What is observed when the protein sample is subjected to Millon’s test? a. Violet interface b. Red precipitate/solution c. Brown/black precipitate d. Yelllow product e. No observable result