Old Javanese legal traditions in pre-colonial Bali

Law codes with their origins in Indic-influenced Old Javanese systems of knowledge comprise an important genre in the Balinese textual record. Written in Kawi—a term encompassing Old Javanese, Middle Javanese and High Balinese—the legal corpus forms a complex and overlapping web of indigenous legal texts and traditions that encompass the codification and administration of civil and criminal justice as well as concepts of morality and right conduct. The most significant codes include the Adhigama, Ku??ram?nawa, P?rw?dhigama, S?rasamuccaya, Swarajambu, Dew?gama (also called Kr?topapati) and Dewadanda. Each of these law codes belongs to a shared tradition of legal thought and practice that is linked to Sanskrit M?navadharma??stra traditions. Manu’s code, most notably the a??ada?awyawah?ra section detailing the eighteen grounds for litigation, was adopted as the model of legal textual principle in the early stages of contact between ancient India and the Indonesian archipelago. Over the course of many centuries, this model informed legal and juridical practice and was adapted and modified to suit indigenous needs. The law codes remained in use in Java until the advent of Islam towards the end of the fifteenth century, and in Bali until the colonial period in the late nineteenth and early twentieth centuries. The Balinese legal textual corpus comprises dozens of interrelated manuscripts, some complete and some fragmentary. They provide significant insights in to pre-colonial judicial practices and forms of government. This article provides a survey of the corpus of legal texts and explores the nature of law in pre-colonial Bali

The Effect of Phosphorylation on the Electron Capture Dissociation of Peptide Ions

The effect of site and frequency of phosphorylation on the electron capture dissociation of peptide ions has been investigated. The ECD of a suite of synthetic peptides (APLSFRGSLPKSYVK; one unmodified, three singly-phosphorylated, three-doubly phosphorylated, and one triplyphosphorylated); two tryptic phosphopeptides (YKVPQLEIVPNpSAEER, α-casein and FQpSEEQQQTEDELQDK, β-casein) and their unmodified counterparts, were determined over a range of ECD cathode potentials. The results show that, for doubly-charged precursor ions, the presence of phosphorylation has a deleterious effect on ECD sequence coverage. The fragmentation patterns observed suggest that for peptides with multiple basic residues, the phospho-groups exist in their deprotonated form and form salt-bridges with protonated amino acid side chains. The fragmentation observed for the acidic tryptic peptides suggested the presence of noncovalent interactions, which were perturbed on phosphorylation. Increasing the ECD electron energy significantly improves sequence coverage. Alternatively, improved sequence coverage can be achieved by performing ECD on triply-charged precursor ions. The findings are important for the understanding of gas-phase fragmentation of phosphopeptides

Separation of cis and trans isomers of polyproline by FAIMS mass spectrometry

High field asymmetric waveform ion mobility spectrometry (FAIMS) is well-established as a tool for separating peptide isomers (sequence inversions and post-translationally modified localization variants). Here, we demonstrate the FAIMS is able to differentiate cis and trans isomers of polyproline. Polyproline assumes an all-cis conformation—the PPI helix—in 1-propanol, and an all-trans conformation—the PPII helix—in aqueous solutions. Differentiation of these conformers may be achieved both through use of a cylindrical FAIMS device and a miniaturized ultrahigh field planar FAIMS device. [Figure: see text] ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s13361-016-1482-1) contains supplementary material, which is available to authorized users

Proteomic Analysis of a Noninvasive Human Model of Acute Inflammation and Its Resolution: The Twenty-one Day Gingivitis Model

The 21-day experimental gingivitis model, an established noninvasive model of inflammation in response to increasing bacterial accumulation in humans, is designed to enable the study of both the induction and resolution of inflammation. Here, we have analyzed gingival crevicular fluid, an oral fluid comprising a serum transudate and tissue exudates, by LC−MS/MS using Fourier transform ion cyclotron resonance mass spectrometry and iTRAQ isobaric mass tags, to establish meta-proteomic profiles of inflammation-induced changes in proteins in healthy young volunteers. Across the course of experimentally induced gingivitis, we identified 16 bacterial and 186 human proteins. Although abundances of the bacterial proteins identified did not vary temporally, Fusobacterium outer membrane proteins were detected. Fusobacterium species have previously been associated with periodontal health or disease. The human proteins identified spanned a wide range of compartments (both extracellular and intracellular) and functions, including serum proteins, proteins displaying antibacterial properties, and proteins with functions associated with cellular transcription, DNA binding, the cytoskeleton, cell adhesion, and cilia. PolySNAP3 clustering software was used in a multilayered analytical approach. Clusters of proteins that associated with changes to the clinical parameters included neuronal and synapse associated proteins

Electron capture dissociation mass spectrometry of phosphopeptides: Arginine and phosphoserine

AbstractWe have previously shown that the presence of phosphorylation can inhibit detection of electron capture dissociation (ECD) fragments of doubly charged peptide ions. The presence of non-covalent interactions, in the form of salt-bridges or ionic hydrogen bonds, prevents the separation of fragments following backbone cleavage. Here, we show the electron capture dissociation mass spectrometry of a suite of model peptides designed to investigate the relationship between phosphoserine and arginine position, namely AApSAnRAmKA (n=0–6, m=6–0), the presence of lysine residues (AApSAAKAARAKA) and AAApSARAAAAKAAAK, and the presence of proline A(A/P)ApSARAAA(A/P)KAAAK. The latter are analogous to the peptides studied previously. The results show that the presence of phosphoserine and basic amino acid residues alone does not inhibit ECD fragmentation, even when the number of basic amino acid residues is greater than the precursor charge state. Neither did the presence of proline in the peptide sequence suppress ECD backbone cleavage. Nevertheless, the presence and relative position of the phosphorylated residue do alter the observed backbone fragmentation abundance. In addition, the presence of phosphorylation appears to inhibit cleavage within the arginine side-chain regardless of the relative position of the arginine residue. The results suggest that ECD fragmentation behaviour is dependent on the three-dimensional structure of a peptide rather than its sequence

Liquid extraction surface analysis field asymmetric waveform ion mobility spectrometry mass spectrometry for the analysis of dried blood spots

LESA mass spectrometry coupled with high field asymmetric waveform ion mobility spectrometry (FAIMS) for the analysis of dried blood spots.</p