1.What type of bonds stabilizes the quaternary structure of proteins? * A. Peptide bond B. Electrostatic interactions C. Hydrogen bonds D. Disulfide bridges E. Hydrophobic bonds 2. A new drug is developed which selectively cleaves covalent bonds between two sulfur atoms of non-adjacent amino acids in a polypeptide chain. Which level of protein structure in affected molecules would be most directly affected by the drug? * A. Primary B. Secondary C. Tertiary D. Quaternary
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- Hello, please help me with my assignment. Can you answer ALL QUESTIONS EXCEPT QUESTIONS 1-31. Which of the following statements is accurate regarding these protein structures?a. Proteins in a quaternary structure consist of a simple polypeptide chain.b. Interactions between the R groups in amino acids form tertiary structure.c. Secondary structures are formed by multiple polypeptide chains.d. The two types of primary structure are α- helices and β- pleated sheets. 2. What type of bonds are formed between amino acids?a. Peptide bondb. Glycosidic linkagec. Hydrogen bondsd. Ester linkages 3. Which of the following is an example of protein denaturation?a. Amino acids fold into repeating patterns due to hydrogen bonding of the peptide backbone.b. Several amino acids are joined together via peptide bonds.c. A protein binds with a substrate, lowering the activation energy of a reaction.d. A protein is exposed to extremely high heat, causing it to lose its secondary structure and be leftwith…Which of the following statements are correct? Explain your answers.A. Proteins are so remarkably diverse because each is made from a unique mixture of amino acids that are linked in random order.B. Lipid bilayers are macromolecules that are made up mostly of phospholipid subunits.C. Nucleic acids contain sugar groups.D. Many amino acids have hydrophobic side chains.E. The hydrophobic tails of phospholipid molecules are repelled from water.F. DNA contains the four different bases A, G, U, and C.Which of the following statement about quaternary structure of protein is correct? Select one: a. Quaternary structure is a force between different polypeptides. b. Hydrogen bond is an only force found in quaternary structure. c. Quaternary structure contains one polypeptide. d. Quaternary structure is an unfolded form of protein.
- 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 resultOnly qno3m I think protein drawing has to show the bond interactions Onlyqno3 solve. I. Given a polypeptide below, answer the following questions: MAGGMIVIIGGMGCNSMVVVIIIGTSSCVIMEMMMIVKII Questions: 1. Enumerate all non-polar amino acids. (Provide the single letter and common name) 2. Enumerate polar amino acids include the acidic and basic types. (Provide the single letter and common name) 3. Illustrate the overall shape of the given polypeptide. Point out the specific side-chain interactions that could occur in this polypeptide by labelling the polypeptide. Defend your answer as to why your polypeptide should assume such final shape. Only accurate drawing needKindly answer questions 7, 8, and 9 please. Put the letter of the answer. 1. Which of the following statements is accurate regarding these protein structures? a. Proteins in a quaternary structure consist of a simple polypeptide chain.b. Interactions between the R groups in amino acids form tertiary structure.c. Secondary structures are formed by multiple polypeptide chains.d. The two types of primary structure are α- helices and β- pleated sheets. 2. What type of bonds are formed between amino acids? a. Peptide bondb. Glycosidic linkagec. Hydrogen bondsd. Ester linkages 3. Which of the following is an example of protein denaturation? a. Amino acids fold into repeating patterns due to hydrogen bonding of the peptide backbone.b. Several amino acids are joined together via peptide bonds.c. A protein binds with a substrate, lowering the activation energy of a reaction.d. A protein is exposed to extremely high heat, causing it to lose its secondary structure and be left with only its…
- Which of the following statements are correct about protein structure (select all that apply)? A. Post-translational modifications such as glycosylation or phosphorylation may alter the structure of a protein B. Only amino acids with a net charge may interact with other amino acids C. The 3D structure of a protein is determined primarily by the protein backbone/main chain conformation while the amino acid sidechains play only a minor role. D. Hydrophobic interactions play a key role in protein folding E. Amino acid sidechains contribute to 3D structure through their ability to form hydrogen bonds with other amino acidsBased on this table: 1) What is the difference between subunit mass and native mass? 2) How do you tell what the likely quarternary structure of the protein is? (heterotrimer, homotrimer, etc.)Which two types of bonding are in the 1ubq (Ubiquitin)? Explain your choices. a) Hydrogen bonding b) Ionic bonding c) Covalent bonding d) Disulfide bonding
- Which of the following is NOT TRUE about secondary structure in proteins? (More than one may apply) A. Stabilized by non-covalent bonds B. Is illustrated by DnaA molecules interacting in the ori C. Unravels at high temperatures when intramolecular non-covalent bonds are destroyed D. Occurs in a subregion of a protein E. Exemplified by beta sheets F. Describes the order of amino acids in a polypeptideLabel: 1) the type of chemical bonds between the amino acids (e.g. covalent bond, ionic bond, metallic bond) 2) the type of interparticle forces of attraction occurring within the protein and with its environment *Indicate at least four observed interparticle forces of attraction *pink - negatively charged, blue - positively charged, yellow - nonpolar and uncharged, green - polar and uncharged *[See example picture] The chemical bond (shown by the arrow) is depicted as a line between the amino acids. Interparticle forces of attraction, such as the one between Phe and Glu (boxed), are not represented by lines but rather by the proximity of amino acids.Which of the following statements about electron microscopy are true? a) Most existing protein structures have been resolved using electron microscopy b) Electron microscopy is not used in structural biology as it can not give as high a resolution as X-ray crystallography and NMR c) The smaller a protein, the easier it is to solve its structure with electron microscopy d) By taking pictures of the same protein frozen in ice thousands of times and then adding them together, you get a high-resolution image of the protein e) The first protein structure with true atomic resolution was solved using electron microscopy last year