The peptide bond is resonance stabilized. What is (are) the direct effect(s) of this on protein structure? This is a multi-select question (select all that apply, it will be marked "right minus wrong"). The R groups of neighbouring amino acid residues lie cis to each other. There is no free rotation about the peptide bond. | The N-H group cannot serve as an H-bond acceptor. Most proteins are hydrophobic. | All six atoms around the bond (including the Ca) lie on the same plane.

Biochemistry
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Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
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Chapter1: Biochemistry: An Evolving Science
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The peptide bond is resonance stabilized. What is (are) the direct effect(s) of this on
protein structure? This is a multi-select question (select all that apply, it will be
marked "right minus wrong").
The R groups of neighbouring amino acid residues lie cis to each other.
| There is no free rotation about the peptide bond.
) The N-H group cannot serve as an H-bond acceptor.
Most proteins are hydrophobic.
| All six atoms around the bond (including the Ca) lie on the same plane.
Transcribed Image Text:The peptide bond is resonance stabilized. What is (are) the direct effect(s) of this on protein structure? This is a multi-select question (select all that apply, it will be marked "right minus wrong"). The R groups of neighbouring amino acid residues lie cis to each other. | There is no free rotation about the peptide bond. ) The N-H group cannot serve as an H-bond acceptor. Most proteins are hydrophobic. | All six atoms around the bond (including the Ca) lie on the same plane.
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