Hydrogen-bond lifetime measured by time-resolved 2D-IR spectroscopy: N-methylacetamide in methanol

Woutersen, Sander; Mu, Yuguang; Stock, Gerhard; Hamm, Peter

doi:10.1016/s0301-0104(01)00224-5

Cited by 282 publications

(346 citation statements)

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“…2 Measurements of the lifetimes of relatively weak hydrogen bonds (< 5 kcal/mol ) at room temperature under thermal equilibrium conditions have recently become possible because of the advent of ultrafast IR techniques. [6][7][8][9][10][11] To the best of our knowledge, no systematic study on the relationship between the lifetimes and strength of hydrogen bonds has been reported.…”

Section: Introductionmentioning

confidence: 99%

Hydrogen Bond Lifetimes and Energetics for Solute/Solvent Complexes Studied with 2D-IR Vibrational Echo Spectroscopy

2007

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Weak π hydrogen bonded solute-solvent complexes are studied with ultrafast two dimensional infrared (2D-IR) vibrational echo chemical exchange spectroscopy, temperature dependent IR absorption spectroscopy, and density functional theory calculations. Eight solute-solvent complexes composed of a number of phenol derivatives and various benzene derivatives are investigated. The complexes are formed between the phenol derivative (solute) in a mixed solvent of the benzene derivative and CCl 4 . The time dependence of the 2D-IR vibrational echo spectra of the phenol hydroxyl stretch is used to directly determine the dissociation and formation rates of the hydrogen bonded complexes. The dissociation rates of the weak hydrogen bonds are found to be strongly correlated with their formation enthalpies. The correlation can be described with an equation similar to the Arrhenius equation. The results are discussed in terms of transition state theory.

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Section: Introductionmentioning

confidence: 99%

Hydrogen Bond Lifetimes and Energetics for Solute/Solvent Complexes Studied with 2D-IR Vibrational Echo Spectroscopy

2007

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“…Spreading spectra into two dimensions increases the spectral resolution, and at the same time allows one to correlate various transitions with each other. The most direct comparison of the two techniques can be made for exchange spectroscopy (EXSY) [16,19,20], for which virtually identical plots have been produced (Fig. 2).…”

Section: Advancing the Sensitivitymentioning

confidence: 99%

Fast infrared spectroscopy of protein dynamics: advancing sensitivity and selectivity

Koziol

Johnson

Stucki-Buchli

et al. 2015

Current Opinion in Structural Biology

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2D-IR spectroscopy has matured to a powerful technique to study the structure and dynamics of peptides, but its extension to larger proteins is still in its infancy, the major limitations being sensitivity and selectivity. Site-selective information requires measuring single vibrational probes at sub-millimolar concentrations where most proteins are still stable, which is a severe challenge for conventional (FT)IR spectroscopy. Besides its ultrafast time-resolution, a so far largely underappreciated potential of 2D-IR spectroscopy lies in its sensitivity gain. The present paper sets the goals and outlines strategies how to use that sensitivity gain together with properly designed vibrational labels to make IR spectroscopy a versatile tool to study a wide class of proteins. Abstract Abstract: 2D-IR spectroscopy has matured to a powerful technique to study the structure

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“…In refs. [85][86][87][88][89] dynamics of the alanine and glycine tripeptides was studied by means of classical molecular dynamics and with the use of semi-empirical potentials (such as GRO-MOS, CHARMM and AMBER). In [90], within the framework of the Hartree-Fock theory, several stable conformations of alanine and glycine tripeptides were found.…”

Section: Introductionmentioning

confidence: 99%

Theory of Phase Transitions in Polypeptides and Proteins

Yakubovich¹

2011

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Hydrogen-bond lifetime measured by time-resolved 2D-IR spectroscopy: N-methylacetamide in methanol

Cited by 282 publications

References 35 publications

Hydrogen Bond Lifetimes and Energetics for Solute/Solvent Complexes Studied with 2D-IR Vibrational Echo Spectroscopy

Hydrogen Bond Lifetimes and Energetics for Solute/Solvent Complexes Studied with 2D-IR Vibrational Echo Spectroscopy

Fast infrared spectroscopy of protein dynamics: advancing sensitivity and selectivity

Theory of Phase Transitions in Polypeptides and Proteins

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