Interaction between an amide nitrogen lone pair and a noncontiguous carbonyl carbon and its effect on amide rotation

Philip S Portoghese, J. G. Turcotte

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

ALTHOUGH rotational barriers1-4 about the C-N bond in simple amides have been investigated extensively by means of nuclear magnetic resonance (NMR) spectroscopy, there is no information about the effect of proximal dipolar groups on the rotational process. Information of this type would be particularly relevant to peptide bonds in proteins because of the multiplicity of dipoles with the potential for Coulombic interaction with the amide moiety, and because such interaction may be important in determining the preferred conformation of proteins5. We have evidence to suggest that N-CO rotation is significantly increased by orbital overlap between the nitrogen atom of the amide group and a noncontiguous carbonyl function.

Original languageEnglish (US)
Pages (from-to)457-459
Number of pages3
JournalNature
Volume230
Issue number5294
DOIs
StatePublished - Dec 1 1971

Fingerprint

Amides
Nitrogen
Carbon
Carbon Monoxide
Magnetic Resonance Spectroscopy
Peptides
Proteins

Cite this

Interaction between an amide nitrogen lone pair and a noncontiguous carbonyl carbon and its effect on amide rotation. / Portoghese, Philip S; Turcotte, J. G.

In: Nature, Vol. 230, No. 5294, 01.12.1971, p. 457-459.

Research output: Contribution to journalArticle

@article{ce96de82c1434f74b95a5255383aab12,
title = "Interaction between an amide nitrogen lone pair and a noncontiguous carbonyl carbon and its effect on amide rotation",
abstract = "ALTHOUGH rotational barriers1-4 about the C-N bond in simple amides have been investigated extensively by means of nuclear magnetic resonance (NMR) spectroscopy, there is no information about the effect of proximal dipolar groups on the rotational process. Information of this type would be particularly relevant to peptide bonds in proteins because of the multiplicity of dipoles with the potential for Coulombic interaction with the amide moiety, and because such interaction may be important in determining the preferred conformation of proteins5. We have evidence to suggest that N-CO rotation is significantly increased by orbital overlap between the nitrogen atom of the amide group and a noncontiguous carbonyl function.",
author = "Portoghese, {Philip S} and Turcotte, {J. G.}",
year = "1971",
month = "12",
day = "1",
doi = "10.1038/230457a0",
language = "English (US)",
volume = "230",
pages = "457--459",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "5294",

}

TY - JOUR

T1 - Interaction between an amide nitrogen lone pair and a noncontiguous carbonyl carbon and its effect on amide rotation

AU - Portoghese, Philip S

AU - Turcotte, J. G.

PY - 1971/12/1

Y1 - 1971/12/1

N2 - ALTHOUGH rotational barriers1-4 about the C-N bond in simple amides have been investigated extensively by means of nuclear magnetic resonance (NMR) spectroscopy, there is no information about the effect of proximal dipolar groups on the rotational process. Information of this type would be particularly relevant to peptide bonds in proteins because of the multiplicity of dipoles with the potential for Coulombic interaction with the amide moiety, and because such interaction may be important in determining the preferred conformation of proteins5. We have evidence to suggest that N-CO rotation is significantly increased by orbital overlap between the nitrogen atom of the amide group and a noncontiguous carbonyl function.

AB - ALTHOUGH rotational barriers1-4 about the C-N bond in simple amides have been investigated extensively by means of nuclear magnetic resonance (NMR) spectroscopy, there is no information about the effect of proximal dipolar groups on the rotational process. Information of this type would be particularly relevant to peptide bonds in proteins because of the multiplicity of dipoles with the potential for Coulombic interaction with the amide moiety, and because such interaction may be important in determining the preferred conformation of proteins5. We have evidence to suggest that N-CO rotation is significantly increased by orbital overlap between the nitrogen atom of the amide group and a noncontiguous carbonyl function.

UR - http://www.scopus.com/inward/record.url?scp=0015228703&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0015228703&partnerID=8YFLogxK

U2 - 10.1038/230457a0

DO - 10.1038/230457a0

M3 - Article

VL - 230

SP - 457

EP - 459

JO - Nature

JF - Nature

SN - 0028-0836

IS - 5294

ER -