
@article {115259,
	title = {Exploring the medicinally important secondary metabolites landscape through the lens of transcriptome data in fenugreek (Trigonella foenum graecum L.).},
	journal = {Sci Rep},
	volume = {12},
	year = {2022},
	month = {2022 Aug 08},
	pages = {13534},
	abstract = {<p>Fenugreek (Trigonella foenum-graecum L.) is a self-pollinated leguminous crop belonging to the Fabaceae family. It is a multipurpose crop used as herb, spice, vegetable and forage. It is a traditional medicinal plant in India attributed with several nutritional and medicinal properties including antidiabetic and anticancer. We have performed a combined transcriptome assembly from RNA sequencing data derived from leaf, stem and root tissues. Around 209,831 transcripts were deciphered from the assembly of 92\% completeness and an N50 of 1382 bases. Whilst secondary metabolites of medicinal value, such as trigonelline, diosgenin, 4-hydroxyisoleucine and quercetin, are distributed in several tissues, we report transcripts that bear sequence signatures of enzymes involved in the biosynthesis of such metabolites and are highly expressed in leaves, stem and roots. One of the antidiabetic alkaloid, trigonelline and its biosynthesising enzyme, is highly abundant in leaves. These findings are of value to nutritional and the pharmaceutical industry.</p>
},
	keywords = {Diosgenin, Hypoglycemic Agents, Plant Extracts, Plants, Medicinal, Transcriptome, Trigonella},
	issn = {2045-2322},
	doi = {10.1038/s41598-022-17779-8},
	author = {Naika, Mahantesha B N and Sathyanarayanan, Nitish and Sajeevan, Radha Sivarajan and Bhattacharyya, Teerna and Ghosh, Pritha and Iyer, Meenakshi S and Jarjapu, Mahita and Joshi, Adwait G and Harini, K and Shafi, K Mohamed and Kalmankar, Neha and Karpe, Snehal D and Mam, Bhavika and Pasha, Shaik Naseer and Sowdhamini, Ramanathan}
}
@article {6136,
	title = {Intramolecular Backbone{\textperiodcentered}{\textperiodcentered}{\textperiodcentered}Backbone Hydrogen Bonds in Polypeptide Conformations. The Other Way Around: ε-Turn.},
	journal = {Biopolymers},
	volume = {108},
	year = {2017},
	month = {01/2017},
	abstract = {<p>In this study, we performed a detailed literature survey of the ε-turn in peptides and proteins. This 3D-structural feature is characterized by an eleven-membered pseudo-cycle closed by an intramolecular backbone{\textellipsis}backbone H-bond. Interestingly, in this motif the direction of the N-H{\textellipsis}O=C H-bond runs opposite to that of the much more popular and extensively investigated α-, β-, and γ-turns. We did not authenticate unequivocally the ε-turn main-chain reversal topology in any linear short peptide. However, it is frequently observed in small cyclic peptides formed by four, five, and six amino acid residues with stringent geometric requirements. Rather surprisingly, ε-turns do occur in proteins, although to a relatively moderate extent, as an isolated feature or in the turn segment of hairpin motifs based on two antiparallel, pleated β-strands. Moreover, the ε-turn may also host not only the seven-membered, intramolecularly H-bonded, pseudo-cycle termed γ-turn, either of the classic or inverse type, but also one (or even two) cis peptide bond(s) or a β-bulge conformation. Based on their ϕ,ψ backbone torsion angles, we were able to classify the protein ε-turns in six different families. Conformational energy computations using the DFT methodology were also performed on the ε-turns adopted by the amino acid triplet -Gly-Gly-Gly- (Gly is the most commonly found residue at each of the three positions in our analysis of proteins). Again, in this computational study, six families of turns were identified, but only some of them resemble rather closely those extracted from our investigation on proteins. This article is protected by copyright. All rights reserved.</p>
},
	issn = {1097-0282},
	doi = {10.1002/bip.22911},
	author = {Toniolo, Claudio and Crisma, Marco and Formaggio, Fernando and Alem{\'a}n, Carlos and Ramakrishnan, Chandrasekharan and Kalmankar, Neha and Balaram, Padmanabhan}
}
