45 research outputs found
FIGURE 1. Bhutanthera fimbriata. A. Flowering plant. B in A new species of Bhutanthera (Orchidaceae; Orchidoideae) from Nepal
No full textFIGURE 1. Bhutanthera fimbriata. A. Flowering plant. B. Flower in front view. C. Lateral sepal. D. Column, ovary and floral bract. E. Dorsal sepal, F. Petal. G. Lip. H. Pollinia. (All drawn by the author from the type specimen.)Published as part of Raskoti, Bhakta Bahadur, 2012, A new species of Bhutanthera (Orchidaceae; Orchidoideae) from Nepal, pp. 57-60 in Phytotaxa 62 (1) on page 58, DOI: 10.11646/phytotaxa.62.1.10, http://zenodo.org/record/506187
FIGURE 1. Sunipia nepalensis. A. Flowering plant. B in A new species of Sunipia (Orchidaceae) from Nepal
No full textFIGURE 1. Sunipia nepalensis. A. Flowering plant. B. Flower (front view). C. Sepal, petal and lip (spread out). D. Floral bract. E. Pedicel and ovary. F. Fruit. G. Operculum. H. Column (side view). I. Pollinarium (all drawn from type specimen by the first author).Published as part of Raskoti, Bhakta Bahadur & Ale, Rita, 2011, A new species of Sunipia (Orchidaceae) from Nepal, pp. 55-58 in Phytotaxa 31 on page 56, DOI: 10.11646/phytotaxa.31.1.2, http://zenodo.org/record/489451
Exploring the relationship between Bhakti, Bhakta, and Yoga in the Prabodhcandroday Nāṭak by Brajvāsīdās
No full textThis chapter attempts to uncover the relationship between bhakti, bhaktas and yoga in the Prabodhcandroday nāṭak by Brajvāsīdās. The author, apparently a Vallabhite, retold the allegorical drama in Brajbhāṣā by blending its own peculiar form of Vedānta with bhakti in the 18th century. I analyse the portrayal of nine characters in the text: eight are personifications of the limbs of Patañjali’s yoga; the ninth is Viṣṇubhakti, embodying devotion to Viṣṇu. My investigation reveals that their portrayals are influenced by Patañjala yoga, by central texts of the Vaishnava traditions, such as the Bhāgavata Purāṇa, as well as by hatha yoga. In addition, bhakti values, such as the company of fellow bhaktas, remain central. I suggest that Brajvāsīdās develops such figures to make space for a non-mainstream bhakta yogi, whom he calls vivekī (discerning person), enriching our understanding of the intersections and interactions of bhakti and yoga in early modern times
Bhaalubhakta's Couplets:FAQ's
No full textAuthor himself has presented himself as Bhaalubhakta; a devotee of Harlot, as a parody to early poet Bhanu Bhakta Acharya of Nepal. It is in honor to Marcus AureliusIn Honor to Marcus Aureliu
Single-Particle Cryo-EM: What happens inside the Black Box?
No full textElectron microscopy has been an important method for visualising biological structures and processes since the 1940s. The discovery of a practical vitreous-ice specimen-preparation technique in the mid-1980s [Adrian 1984] led to modern-day Cryogenic Electron Microscopy (Cryo-EM) which in recent years has become a major technique for studying the architecture of biological macromolecules. Many further instrumental and data-analysis improvements were established in the decades after the introduction of the “vitreous-ice” state of water. Especially the advent of direct electron detectors boosted the quality of the recorded data, allowing atomic-resolution information of biological complexes to be harvested in the early 2010s, developments that truly revolutionized the use of Cryo-EM in structural biology. Single-Particle Analysis (SPA) of isolated molecules, prepared in a thin layer of vitreous water, has proven a most successful approach in structural biology and now often supplants the use of classical techniques like X-ray crystallography, especially for large biological complexes. The ever-increasing number of researchers using Cryo-EM is reflected by the growing number of depositions in the Electron Microscopy Data Bank (EMDB). Explaining this methodology to a new generation of researchers has now become a priority. In writing this review we were reminded of some persistent confusions that emerged in the early days of Cryo-EM but that continue to muddle the field. A new problem with the prolific use of Graphic User Interfaces (GUIs), is that the underlying methodology is often no longer transparent to the users of these “black boxes”. Complicated procedures, well hidden behind a GUI window, may contain methodological flaws that the user must be aware of. The conquering of markets in this booming Cryo-EM field – crucial for developing new pharmaceuticals – must not prevail over scientific integrity. We here describe and critically review the principles of single-particle Cryo-EM. We warn for procedures that have gone astray and could generate serious problems especially in the quality-control of Single-Particle Cryogenic Electron Microscopy
Mechanistic Insight into the Reactivation of BCAII Enzyme from Denatured and Molten Globule States by Eukaryotic Ribosomes and Domain V rRNAs.
No full textIn all life forms, decoding of messenger-RNA into polypeptide chain is accomplished by the ribosome. Several protein chaperones are known to bind at the exit of ribosomal tunnel to ensure proper folding of the nascent chain by inhibiting their premature folding in the densely crowded environment of the cell. However, accumulating evidence suggests that ribosome may play a chaperone role in protein folding events in vitro. Ribosome-mediated folding of denatured proteins by prokaryotic ribosomes has been studied extensively. The RNA-assisted chaperone activity of the prokaryotic ribosome has been attributed to the domain V, a span of 23S rRNA at the intersubunit side of the large subunit encompassing the Peptidyl Transferase Centre. Evidently, this functional property of ribosome is unrelated to the nascent chain protein folding at the exit of the ribosomal tunnel. Here, we seek to scrutinize whether this unique function is conserved in a primitive kinetoplastid group of eukaryotic species Leishmania donovani where the ribosome structure possesses distinct additional features and appears markedly different compared to other higher eukaryotic ribosomes. Bovine Carbonic Anhydrase II (BCAII) enzyme was considered as the model protein. Our results manifest that domain V of the large subunit rRNA of Leishmania ribosomes preserves chaperone activity suggesting that ribosome-mediated protein folding is, indeed, a conserved phenomenon. Further, we aimed to investigate the mechanism underpinning the ribosome-assisted protein reactivation process. Interestingly, the surface plasmon resonance binding analyses exhibit that rRNA guides productive folding by directly interacting with molten globule-like states of the protein. In contrast, native protein shows no notable affinity to the rRNA. Thus, our study not only confirms conserved, RNA-mediated chaperoning role of ribosome but also provides crucial insight into the mechanism of the process
Lifting of vector-valued automorphic forms
No full textRecently, the first author [1] showed that the admissible vector-valued
automorphic forms lift to the admissible ones. In this article, we study the
lifts for the logarithmic vector-valued automorphic forms and explicitly
compute the Fourier coefficients of the lifted vector-valued automorphic forms.Comment: 20 pages, revised following referee's suggestion
Denaturant-induced unfolding of BCAII.
No full text(A) Tryptophan fluorescence of native (orange) and denatured (green) Bovina Carbonic Anhydrase II (BCAII) shows reduction in fluorescence intensity upon denaturation. In the inset a cartoon representation of the crystal structure of BCAII enzyme (PDB code 1V9E) is shown with the tryptophan residues highlighted in red stick. (B) Emission spectra (320–600) of the extrinsic fluorescence of native, fully unfolded (unf+EDTA; unf-EDTA) and molten globule (MG+EDTA;MG-EDTA) BCAII recorded using 8-anilinonaphthalene-1-sulphonic acid (ANS) dye showing considerably higher binding of ANS with molten globule BCAII compared to native or unfolded BCAII. (C) Crystal structure of BCAII enzyme (PDB code 1V9E) having a diameter of ~5nm with its secondary structures highlighted in different colors. Under different conditions, change in the hydrodynamic diameter of native BCA upon denaturation to molten globule-like (~80% population 10nm in 1.5 M GuHCl without EDTA (brown), 100% population 18 nm in 1.5 M GuHCl with EDTA (pink)) and fully unfolded state (~60% population 27 nm in 6 M GuHCl with or without EDTA (blue)) is shown as obtained from dynamic light scattering (DLS) experiments (the experiment was repeated twice for each case, acquiring data twice each time).</p
Binding analysis of BCAII in denatured and native states with the eukaryotic rRNA.
No full textSensogram recorded when varying concentrations of protein (in fully denatured state (A) and native state (B)) were injected over the RNA immobilized on the streptavidin chip. Binding profile of fully denatured BCAII with LdV (A) and YdV (B) shows unusually steep association pattern indicating very fast mode of interaction. The experiment with denatured protein was done in low temperature. No notable concentration dependent increase in binding is observed for native BCAII with either LdV (C) or YdV (D) indicating no significant affinity of the native protein towards RNA.</p
Eukaryotic ribosomal RNA domain V-mediated folding of denatured BCAII.
No full textSecondary structure diagram of 3’end of the LSU-RNA of T. brucei with the domain V (highlighted in yellow) (A) and the same of S. cerevisiae (B). The peptidyl transferase centre (PTC) in domain V is marked with arrows in (A and B). (C) BCAII reactivation by the domain V RNA of L. donovani (LdV) and S. cerevisiae (YdV) shows ~65% activity recovered. RN and RS represent the same as in Fig 1. Statistical significance is shown by ** (p D) Time course of reactivation of BCAII by domain V RNA from S. cerevisiae (▪) and L. donovani (•) shows faster reactivation for S. cerevisiae.</p
