Title: Polymorphism of L-Tryptophan: data

Citation
Al Rahal O, Hughes CE, Williams PA, et al. (2019). Polymorphism of L-Tryptophan: data. Cardiff University. http://doi.org/10.17035/d.2019.0085816490


Access Rights: Data is provided under a Creative Commons Attribution (CC BY 4.0) licence
Access Method: Click to email a request for this data to opendata@cardiff.ac.uk

Dataset Details
Publisher: Cardiff University
Date (year) of data becoming publicly available: 2019
Data format: .xlsx, .raw, .cpi, .asc
Software Required: Excel
.raw: Bruker software "EVA"
.cpi and .asc: Various free software for PXRD data.
.txt: Generated by the Bruker software "TopSpin"

Estimated total storage size of dataset: Less than 100 megabytes
DOI: 10.17035/d.2019.0085816490

Description

A new polymorph of L‑tryptophan has been prepared by crystallization from the gas phase, with structure determination carried out directly from powder XRD data augmented by periodic DFT-D calculations. The new polymorph (denoted β) and the previously reported polymorph (denoted α) are both based on alternating hydrophilic and hydrophobic layers, but with substantially different hydrogen-bonding arrangements. The β polymorph exhibits the energetically favourable L2-L2 hydrogen-bonding arrangement, which is unprecedented for amino acids with aromatic side-chains; the specific molecular conformations adopted in the β polymorph facilitate this hydrogen-bonding scheme while avoiding steric conflict of the side-chains.

Data presented is the powder XRD on the new polymorph over a range of temperatures, NMR data on the new polymorph and results from DFT-D calculations of the stabilities of the two forms.

Researhc results based upon these data are published at https://doi.org/10.1002/anie.201908247



Keywords

solid-state nuclear magnetic resonance, XRD

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Last updated on 2020-03-02 at 14:58