Help me pleaseeee pots Which of the following non-covalent interactions is the driving force in theinitial determination of protein tertiary structure: a. ionic interactions b. hydrogenbonding c. London forces d. hydrophobic interactions e. none.008 To

A protein's function depends on its structure. There are four levels of protein structure: primary,…

Answered: po Which of the following non-covalent…

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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Describe the levels of structure of a protein and tell how they would be affected by: a. Hydrolysis with 6M HCl (breaks peptide bond)b. Heating with mercaptoethanol (breaks hydrogen bonds)
Which of the following is not true about the properties of a peptide (amide) bond? a.The bond order of the peptide bond is 2 b.The bond is in resonance which makes it (and the 6 atoms around it and included within it) planar c.Delocalization of electrons through the peptide bond contributes to a net dipole for the bond d.Peptide bonds are very, very strongly favored to be in the trans conformation, but proline is an exception because it is more isoenergetic due to its sidechain ring, and can be cis.
Which of the following is incorrect concerning protein structure determination by X-ray crystallography? Choose one: O A. X-ray crystallography provides dynamic information about protein structure. O B. A 1.5 Å resolution structure is better than a 3 Å resolution structure. O C. Isomorphous replacement is used to aid phase determination. O D. Highly ordered crystals are required.
All of the following are considered “weak” interactions in proteins, except: a. hydrogen bonds. b. hydrophobic interactions. c. ionic bonds. d. peptide bonds. e. van der Waals forces.
4.1. From this structure, what is the predominant secondary structure of the protein? 4.2. Based on what you can observe from the protein, what is its highest level of organizational structure? 4.3. If applicable, how many subunits does this protein have and are they identical? 4.4. If electrostatic interactions primarily stabilize this structure, propose a method to test your observations in 4.2 and 4.3. I
Which of the following statements is incorrect? A.- the structure and charge of the proteins have direct effects on the rate of its migration through the gel matrix include b.- SDS is a type of a buffer with strong protein-denaturing effect and binds to the protein backbone at a constant molar ratio c.- SDS and polyacrylamide gel largely eliminates the influence of the structure and charge, and proteins are separated solely based on polypeptide chain length. d.When proteins are separated by electrophoresis through a gel matrix, smaller proteins appears at the lower portion of the gel
Which of the following most directly applies to the formation of the secondary structures of proteins? A B с D formation of ionic bonds between the R groups of two polypeptides formation of nonpolar interactions between two R groups on the same polypeptide formation of covalent bonds via dehydration reactions between two amino acids formation of hydrogen bonds between between amino and carboxyl groups
The following protein crystal structure is the Human Serum Albumin complexed with octadecanoic acid (PDB ID: 1E7I). According to the protein data bank, Human Serum Albumin is composed of 72% helical structure. Among the following options (a-c), select the possible Ramachandran plot for the above Human Serum Albumin. (a) (b) (c) Phi Phi Phi
Which of the following statements are correct about the native state of a protein (select all that apply)? A. Polar sidechains commonly interact with water B. Hydrophobic amino acids tend to be on surface of protein C. The sidechains of polar amino acids are most commonly found in the central core of a protein D. Formation of an alpha-helix is primarily driven by hydrogen bonds between the protein main chain, not sidechains. E. Secondary structure is largely driven by hydrophobic interactions
Which of the following compounds is most similar to the transition state of peptide bond hydrolysis? A. R2 D. R2- H HO .R1 N میں ملی B. R2 مل ما -R1 E. OH R2 C -R1
Draw the following amino acids interactions: 1. H-bond - between -0H of Serine amino acid and C=0 backbone of glutamic acid. 2. Ionic bond- between ionized aspartic and asparagine amino acids. 3. Disulfide interaction between 2 molecules of Cysteine amino acids. 4. Hydrophobic interaction between Alanine and Leucine R-groups.
A major interaction that stabilize tertiary structures of proteins is O a. electrostatic interaction O b. all of the three types O c. hydrophobic interaction O d. disulfide bond

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po Which of the following non-covalent interactions is the driving force in the initial determination of protein tertiary structure: a. ionic interactions b. hydrogen bonding c. London forces d. hydrophobic interactions e. none.008 Tom, a