In the following diagram of a portion of a protein, label the types of interactions that are shown.What level of protein structure are these interactions producing? b.CHCH2|- PolypeptidebackboneCH3H;C CH3CHС —ОН-CH2-S-SCH,-а.|CH2с.-CH2-CH2-CH2-CH2¬NH3* O-C–CH,-d..

The structural organization of protein was classified into four different levels and they are…

Answered: b. CH CH2 | H;Č CH3 - Polypeptide…

Science

Biochemistry

b. CH CH2 | H;Č CH3 - Polypeptide backbone H3C CH3 ! CH C=OH -CH2+S-S CH2– а. CH2 -CH2-CH2-CH2–CH2-NH;* 0-C-CH2- d.

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

See similar textbooks

Similar questions

The following figure is a diagram (cartoon or caricature) of the structure of a protein. What types of secondary structure are observed in the molecule? Is it a globular protein or a fibrous one?
The following is an example of which level of protein structure? What bonds form this level of structure? Asp-Met-Leu-Trp-Gly-Asn-Lys
do a and e please and For e, choose two types of interactions, and then give an example of the amino acids in this polypeptide that would interact together in that way.
Which of the following is true about the relative position of hydrophilic and hydrophobic amino acids in globular protein structures in aqueous solutions? Hydrophobic amino acids tend to be found in the core, while hydrophilic amino acids tend to be on the outer surface of proteins. Hydrophilic amino acids tend to be found in the core, while hydrophobic amino acids tend to be on the outer surface of proteins. There is an even distribution of hydrophobic and hydrophilic amino acids between the inner core and outer surface of proteins. There is no predictable distribution of hydrophilic and hydrophobic amino acids; it depends on the specific protein
1.0.1 mL of a protein solution of concentration of 11 mg/mL was diluted to a total volume of 4.0 mL with water (i.e. 0.1 mL of the solution was added to 3.9 mL of water). 2 mL of this solution was then mixed with 18 mL of water. What is the concentration of the diluted protein solution? Space to show your workings:
Protein structures have several different levels of organization. In the space below indicate the type of molecular bonds that can contribute to each level of organization: primary- secondary- tertiary- quarternary-
Match the protein structure terms on the left with the descriptions on the right. v (Choose ) commonly observed combinations of secondary structural elements tertiary structure Long segments of secondary structure. supersecondary structure basic component of quaternary structure Spatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the peptide Spatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the side chain compact structural or functional regions within a given polypeptide functional structures formed by non-covalent interactions between multiple polypeptides. domain (Choosel subunit quaternary structure (Choose)
The tertiary structure of a protein is the 3-dimensional folding of the polypeptide chain. What types of bonds support the folding of proteins into this level of protein structure? Also, how do these bonds/interactions impact how a protein folds and its surface properties? Can the tertiary structure of a protein depend on the type of cell system used for synthesis? Explain.
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
Levels of structure in a protein (primary, secondary, tertiary, quaternary): What each of these refers to? Differences in how secondary and tertiary structure form?
Explain the role of hydrophobic exclusion during protein folding (tertiary structure); what type of aminoacids would you find towards the center of the protein? Charged? Polar? Non-polar
A mutation leads to a change in amino acid from valine, an amino acid with a nonpolar side chain, to aspartic acid, an amino acid with a polar, negatively-charged side chain. Do you think that the following levels of protein structure change? If so, how and why? If not, why not? Please frame your answer in terms of chemical bonds and interactions. (primary structure, secondary structure, tertiary structure, quartenary structure)