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Lavina C. Snoek

Researcher at University of Oxford

Publications -  29
Citations -  2065

Lavina C. Snoek is an academic researcher from University of Oxford. The author has contributed to research in topics: Hydrogen bond & Conformational isomerism. The author has an hindex of 25, co-authored 29 publications receiving 1985 citations. Previous affiliations of Lavina C. Snoek include Fritz Haber Institute of the Max Planck Society & German Cancer Research Center.

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Conformational landscapes in amino acids: infrared and ultraviolet ion-dip spectroscopy of phenylalanine in the gas phase

TL;DR: In this article, a full structural assignment of the most stable conformers of phenylalanine, based upon a combination of ultraviolet and infrared ion-dip spectroscopy of the jet-cooled amino acid, coupled with high-level ab initio computation is presented for the first time.
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Conformational landscapes of aromatic amino acids in the gas phase : infrared and ultraviolet ion dip spectroscopy of tryptophan

TL;DR: The conformational structures of tryptophan, isolated in the gas phase, have been assigned by combining the results of ultraviolet hole-burning and infrared ion dip spectroscopy with the predictions of ab initio calculations conducted at the MP2/6-311 + G(d,p)//B3LYP/6 −31 + G (d) levels of theory as discussed by the authors.
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Hydrogen bonding and cooperativity in isolated and hydrated sugars: mannose, galactose, glucose, and lactose

TL;DR: The conformation of phenyl-substituted monosaccharides and their singly hydrated complexes is investigated in the gas phase by means of a combination of mass selected, conformer specific ultraviolet and infrared double resonance hole burning spectroscopy experiments, and ab initio quantum chemistry calculations.
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Infrared fingerprint spectroscopy and theoretical studies of potassium ion tagged amino acids and peptides in the gas phase.

TL;DR: Infrared multiple-photon dissociation spectroscopy is effected on the K(+) tagged aromatic amino acids tyrosine and phenylalanine, as well as the K (+) tagged peptides bradykinin fragment 1-5 and [Leu]-enkephalin to determine whether the complex is in the charge solvation (CS) or salt bridge (SB) configuration.
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A spectroscopic and computational exploration of tryptophan–water cluster structures in the gas phase

TL;DR: In this paper, mass-selected R2PI spectra of hydrated tryptophan clusters, generated through thermal evaporation into an expanding moist argon jet, have been recorded and analysed using ultra-violet hole-burn and infra-red ion dip spectroscopy, and interpreted in the light of a series of ab initio calculations for singly, doubly and triply hydrated structures.