Select the CORRECT description of the peptide bond. The peptide bond can freely rotate around the peptide bond. The peptide bond is non-polar, hydrophobic and does not have a dipole. The peptide bond is most stable in the cis configuration. The peptide bond is rigid and planar. The peptide bond has a mix of single and double bond characters. The peptide bond is most stable in the trans configuration.

Select the CORRECT description of the peptide bond. The peptide bond can freely rotate around the peptide bond. The peptide bond is non-polar, hydrophobic and does not have a dipole. The peptide bond is most stable in the cis configuration. The peptide bond is rigid and planar. The peptide bond has a mix of single and double bond characters. The peptide bond is most stable in the trans configuration.

Nutrition Now

8th Edition

ISBN:9781337415408

Author:Brown

Publisher:Brown

Chapter15: Proteins And Amino Acids

Section: Chapter Questions

Problem 12RQ

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How many peptide bonds are present in the peptide shown below?
Drag each of the following items into the corresponding boxes to indicate the protein structural level that is predominantly affected by the chemical interactions listed. Some items may be placed in more than one box. Reset Help Hydrogen bonds between polar groups in amino acid side chains Hydrophobic interactions between amino acid side chains lonic bonds between positively- charged and negatively-charged amino acid side chains Peptide bonds Hydrogen bonds between carbonyl oxygens and amino nitrogens within a polypeptide backbone Disulfide bonds Primary structure Seconday structure Tertiary structure Quaternary structure
the resonance stabilization of the amide linkage has profound effects on protein structure. Which of the following are the direct effect(s) of this on protein structure? Select all that apply All six atoms around the bond (including the Co) lie on the same plane There is no free rotation about the peptide bond. The bond between the carbon and the nitrogen in the peptide bond keeps "flickering" between being a single bond and a double bond. The peptide bond is polar. The nitrogen in the peptide bond cannot accept a hydrogen bond.
In the peptide shown below, a covalent bond that could rotate to form secondary structure is correctly identified/labeled by letter: с E OH Thill find -OH HN NH "NH₂
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)
What two chemical groups are involved in the formation of a peptide bond?
This image shows the tertiary structure of a protein segment. Tertiary structure results from different interactions, or forces, between groups. Move the example of each force to the appropriate description on the protein. Then, identify the major force controlling tertiary structure. (Need help) It says I'm wrong.
The following shows a protein with mostly beta sheet secondary structures. Which force stabilizes the beta sheet secondary structure of proteins? hydrophobic interactions between nonpolar amino acid side chains within the protein. electrostatic interactions between lysine and aspartic acid residues within the protein. hydrogen bonding between hydrogen bond donors and hydrogen bond acceptors of the peptide backbone. covalent disulfide linkages between cysteine residues within the protein.
In the peptide shown below, a covalent bond that could rotate to form secondary structure is correctly identified / labeled by letter: A B OH still fot D OB OC O O O B D F C OA HN E NH OH "NH₂ - F
The dihedral or torsion angles of polypeptide backbone, the allowed values of which are summarized by the Ramachandran diagram, refer to rotation of the following pair of bonds. Cα-N and Cα-R C=O and Cα-N C-N and Cα-C Cα-C and Cα-N Cα-R and Cα-C
Draw the structure of the following polypeptide at physiological pH. You do not need to indicate the names or abbreviations. Also highlight the phi and psi bonds around the third amino acid. Protein sequence: PARTICLE Protein sequence: NEDSTARK
The sequence of a peptide is given below. Ala-gly-val-leu-trp-lys-ser-phe-arg-proWhich peptide bond(s) are cleaved by chymotrypsin(

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	The peptide bond can freely rotate around the peptide bond.
	The peptide bond is non-polar, hydrophobic and does not have a dipole.
	The peptide bond is most stable in the cis configuration.
	The peptide bond is rigid and planar.
	The peptide bond has a mix of single and double bond characters.
	The peptide bond is most stable in the trans configuration.