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1.
J Forensic Odontostomatol ; 37(1): 51-62, 2019 May 01.
Article in English | MEDLINE | ID: mdl-31187743

ABSTRACT

Dental forensics for the resolution of unnatural death remains an underdeveloped field. Accordingly, an experimental study was conducted with six to seven months old Wistar rats that were drowned in order to identify key postmortem features and pattern of dental decomposition. The visual, structural and elemental changes were assessed periodically. Based on mode of death, they were designated as SB (euthanized and soil buried), FWD (fresh water drowned) and SWD (sea water drowned). Postmortem features as well as the structural and elemental patterns of decomposition of teeth were analyzed with Field Emission Scanning Electron Microscopy (FE-SEM) and Energy Dispersive Spectroscopy (EDAX) periodically for two months. The periodic observation of elemental changes in the teeth of SB, FWD and SWD rats allowed us to derive an equation using linear regression analysis to relate the degree of dental decomposition with the time since death. The difference in pattern of surface deterioration was also observed. The present findings could provide a better knowledge in resolving unnatural deaths and supporting evidence for legal prosecution.


Subject(s)
Drowning/pathology , Incisor/pathology , Postmortem Changes , Animals , Burial , Forensic Dentistry/methods , Fresh Water , Linear Models , Microscopy, Electron, Scanning , Models, Animal , Pilot Projects , Rats, Wistar , Seawater , Spectrometry, X-Ray Emission
2.
Analyst ; 140(13): 4558-65, 2015 Jul 07.
Article in English | MEDLINE | ID: mdl-26040325

ABSTRACT

Phospholipids are important membrane components involved in diverse biological activities ranging from cell signaling to infection by viral particles. A thorough understanding of protein-phospholipid interaction dynamics is thus crucial for deciphering basic cellular processes as well as for targeted drug discovery. For any specific phospholipid-protein binding experiment, various groups have reported different binding constants, which are strongly dependent on applied conditions of interactions. Here, we report a method for accurate determination of the binding affinity and specificity between proteins and phospholipids using a model interaction between PLC-δ1/PH and phosphoinositide phospholipid PtdIns(4,5)P2. We developed an accurate Force Distance Spectroscopy (FDS)-based assay and have attempted to resolve the problem of variation in the observed binding constant by directly measuring the bond force. We confirm the FDS findings of a high bond strength of ∼0.19 ± 0.04 nN by Surface Plasmon Resonance (SPR) data analysis, segregating non-specific interactions, which show a significantly lower K(D) suggesting tight binding.


Subject(s)
Blood Proteins/chemistry , Blood Proteins/metabolism , Microscopy, Atomic Force/methods , Phosphatidylinositol 4,5-Diphosphate/metabolism , Phosphoproteins/chemistry , Phosphoproteins/metabolism , Surface Plasmon Resonance/methods , Kinetics , Protein Binding , Protein Structure, Tertiary
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