Conformational analysis and intramolecular interactions in 2-haloethanols and their methyl ethers

Souza, Felipe Rodrigues de; Freitas, Matheus P.

doi:10.1016/j.comptc.2010.12.014

Cited by 21 publications

(24 citation statements)

References 24 publications

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“…This completely agrees with the results of theoretical work [35], OH ν OH 0 ν σ OH * according to which intramolecular HB of 2 haloetha nols is mainly ensured by electrostatic interactions, and the contribution of specific interactions increases in the series F < Cl < Br < I.…”

Section: Resultssupporting

confidence: 91%

The bellamy relationship and the nature of the H-bond. 2-Haloethanols

Вокин

Turchaninov

2015

Opt. Spectrosc.

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IR spectroscopy data show that the intramolecular H bond in alcohols with the general formula XCH 2 CH 2 OH (X = F, Cl, Br) in a solution is mainly of a nonspecific nature. Molecules of 2 haloethanol form three center complexes with an external H bond acceptor. The intramolecular component of their bifurcated bond causes a stronger spectroscopic effect as compared to the two center H bond of ethanol or 1 propanol.

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Section: Resultssupporting

confidence: 91%

The bellamy relationship and the nature of the H-bond. 2-Haloethanols

Вокин

Turchaninov

2015

Opt. Spectrosc.

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“…Hydrogen bonding, often described as an electrostatic dipole-dipole interaction, is one of the significant driving forces in protein folding, [66] contributes to the formation of a respectively distinct conformation of peptides/proteins. [67] As mentioned, negatively charged amino acids D and E are much closer to each other in the sequence of YEQ2Q3. It is this electrostatic repulsion interaction that drives the formation of the stretched and extended state with fewer hydrogen bonds as stable structure for YEQ2Q3.…”

Section: Resultsmentioning

confidence: 85%

Single‐Molecule Study of Peptides with the Same Amino Acid Composition but Different Sequences by Using an Aerolysin Nanopore

Angelov

et al. 2020

ChemBioChem

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Nanopores are original sensors employed for highly sensitive peptides/proteins detection. Herein, we describe the use of an aerolysin nanopore to identify two similar model peptides, YEQYEQQDDDRQQQ (YEQ2Q3) and QDDDRQQQYEQYEQ (Q3YEQ2), with the same amino acid composition but different sequences. All‐atom molecular dynamics (MD) simulations reveal that YEQ2Q3 possesses fewer hydrogen bonds and a more extended conformation than Q3YEQ2. These two peptides, which fold differently, exhibit obviously distinct mass‐independent current blockades with characteristic dwell times when entering the aerolysin nanopore. Typically, at +60 mV, the statistical dwell time of 0.630±0.018 ms for peptide Q3YEQ2 is four times longer than the value of 0.160±0.001 ms for peptide YEQ2Q3, and yet peptide YEQ2Q3 induces ∼1.9 % larger blockade current amplitude than peptide Q3YEQ2. The obtained results show the remarkable potential of aerolysin nanopore for peptides/proteins identification, characterization, sequencing and also demonstrate that the mass identification of nonuniformly charged peptides/proteins by using the nanopore technique could be complicated by their folded structure and complex analyte‐pore interaction.

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“…Each minimum was subsequently optimized at the MP2/aug-cc-pVDZ level, and the respective energies are given in Table 1, which shows that the conformer of 5 with the hydroxy hydrogen directed toward the fluorine atom (θ = 330.0°) is the most stable structure in the gas phase (this structure will be further referred to as the global minimum ). This suggests that a F∙∙∙HO intramolecular HB is operating and governs the stability of 5 ; however, different organofluorine compounds with similar orientation of the hydroxy group do not exhibit such an interaction and are highly stable [6,8]. This can be either due to other attractive interactions present in the referred conformer or prevalent repulsive interactions (e.g., between fluorine and oxygen lone pairs) in the other conformer(s).…”

Section: Resultsmentioning

confidence: 99%

Conformational analysis, stereoelectronic interactions and NMR properties of 2-fluorobicyclo[2.2.1]heptan-7-ols

Rezende

Moreira²,

Cormanich³

et al. 2012

Beilstein J. Org. Chem.

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SummaryFour diastereoisomers of 2-fluorobicyclo[2.2.1]heptan-7-ols were computationally investigated by using quantum-chemical calculations, and their relative energies were analyzed on the basis of stereoelectronic interactions, particularly the presence or otherwise of the F∙∙∙HO intramolecular hydrogen bond in the syn-exo isomer. It was found through NBO and AIM analyses that such an interaction contributes to structural stabilization and that the 1h J F,H(O) coupling constant in the syn-exo isomer is modulated by the n F→σ*OH interaction, i.e., the quantum nature of the F∙∙∙HO hydrogen bond.

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Conformational analysis and intramolecular interactions in 2-haloethanols and their methyl ethers

Cited by 21 publications

References 24 publications

The bellamy relationship and the nature of the H-bond. 2-Haloethanols

The bellamy relationship and the nature of the H-bond. 2-Haloethanols

Single‐Molecule Study of Peptides with the Same Amino Acid Composition but Different Sequences by Using an Aerolysin Nanopore

Conformational analysis, stereoelectronic interactions and NMR properties of 2-fluorobicyclo[2.2.1]heptan-7-ols

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