Preparation of Nuclear Spin Singlet States using Spin-Lock Induced Crossing [PDF]
Phys. Rev. Lett. 111, 173002 (2013), 2013 We introduce a broadly applicable technique to create nuclear spin singlet states in organic molecules and other many-atom systems. We employ a novel pulse sequence to produce a spin-lock induced crossing (SLIC) of the spin singlet and triplet energy levels, which enables triplet/singlet polarization transfer and singlet state preparation.
arxiv +1 more source
In-situ measurements of the radiation stability of amino acids at 15-140 K [PDF]
2012, Icarus 220, 647-659, 2015 We present new kinetics data on the radiolytic destruction of amino acids measured in situ with infrared spectroscopy. Samples were irradiated at 15, 100, and 140 K with 0.8-MeV protons, and amino-acid decay was followed at each temperature with and without H$_2$O present.
arxiv +1 more source
Phenylalanine iminoboronates as new phenylalanine hydroxylase modulators
RSC Adv., 2014 Herein we report the discovery of new modulators of human phenylalanine hydroxylase (hPAH) inspired by the structure of its substrate and regulatorl-phenylalanine.
Rita C. Guedes +7 more
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Probing Scalar Coupling Differences via Long-Lived Singlet States [PDF]
, 2015 We probe small scalar coupling differences via the coherent interactions between two nuclear spin singlet states in organic molecules. We show that the spin-lock induced crossing (SLIC) technique enables the coherent transfer of singlet order between one spin pair and another.
arxiv +1 more source
Electronic decoherence following photoionization: full quantum-dynamical treatment of the influence of nuclear motion [PDF]
Physical Review A 95, 033425 (2017), 2017 Photoionization using attosecond pulses can lead to the formation of coherent superpositions of the electronic states of the parent ion. However, ultrafast electron ejection triggers not only electronic but also nuclear dynamics---leading to electronic decoherence, which is typically neglected on time scales up to tens of femtoseconds.
arxiv +1 more source
Deciphering the 'fuzzy' interaction of FG nucleoporins and transport factors using SANS [PDF]
Structure 2018 26 477-84, 2017 The largely intrinsically disordered phenylalanine-glycine-rich nucleoporins (FG Nups) underline a selectivity mechanism, which enables the rapid translocation of transport factors (TFs) through the nuclear pore complexes (NPCs). Conflicting models of NPC transport have assumed that FG Nups undergo different conformational transitions upon interacting ...
arxiv +1 more source
Integrated molar absorptivity of mid- and far-infrared spectra of glycine and other selected amino acids [PDF]
, 2020 A selection of five proteinogenic amino acids, namely glycine, isoleucine, phenylalanine, tyrosine and tryptophan were studied in the mid-infrared and in the far-infrared with the purpose to facilitate the search and identification of these astrobiological and astrochemical relevant molecules in space environments.
arxiv +1 more source
pH Dependent surface enhanced Raman study of Phe + Ag Complex and DFT calculations for spectral analysis [PDF]
, 2006 Surface enhanced Raman spectra of Phenylalanine (Phe) in Ag colloidal solution have been recorded for Phe solutions of different pH. Spectral line-shape analyses of the enhanced modes, at 1005, 1380 and 1582 cm-1, between pH 4.5 and 10.5, have been carried out. The variation of spectral line-width with pH reveals two possible mechanisms in solution: (i)
arxiv +1 more source
ProtVec: A Continuous Distributed Representation of Biological Sequences [PDF]
PLoS ONE 10(11): e0141287, 2015, 2015 We introduce a new representation and feature extraction method for biological sequences. Named bio-vectors (BioVec) to refer to biological sequences in general with protein-vectors (ProtVec) for proteins (amino-acid sequences) and gene-vectors (GeneVec) for gene sequences, this representation can be widely used in applications of deep learning in ...
arxiv +1 more source
Direct evidence for a phenylalanine site in the regulatory domain of phenylalanine hydroxylase [PDF]
Archives of Biochemistry and Biophysics, 2011 The hydroxylation of phenylalanine to tyrosine by the liver enzyme phenylalanine hydroxylase is regulated by the level of phenylalanine. Whether there is a distinct allosteric binding site for phenylalanine outside of the active site has been unclear. The enzyme contains an N-terminal regulatory domain that extends through Thr117. The regulatory domain
Andrew P. Hinck +4 more
openaire +3 more sources