KEANEKARAGAMAN JENIS BURUNG DI TAMAN NASIONAL BANTIMURUNG BULUSARAUNG, SULAWESI SELATAN

Bantimurung Bulusaraung National Park is an important protected area in Sulawesi. This area has a high ornithological value because it holds many Sulawesi’s endemic species. Bird surveys using MacKinnon species lists and point count were conducted in three types of habitat in Bantimurung and Balocci from 23 February to 7 March 2011 and a total of 57 species were recorded, with the highest number of species found in Balocci Resort. Sixteen species were Sulawesi’s endemic. Keywords: Bantimurung Bulusaraung National Park, birds’ biodiversit

Supplement: "Localization and broadband follow-up of the gravitational-wave transient GW150914" (2016, ApJL, 826, L13)

This Supplement provides supporting material for Abbott et al. (2016a). We briefly summarize past electromagnetic (EM) follow-up efforts as well as the organization and policy of the current EM follow-up program. We compare the four probability sky maps produced for the gravitational-wave transient GW150914, and provide additional details of the EM follow-up observations that were performed in the different bands

Localization and Broadband Follow-up of the Gravitational-wave Transient GW150914

A gravitational-wave (GW) transient was identified in data recorded by the Advanced Laser Interferometer Gravitational-wave Observatory (LIGO) detectors on 2015 September 14. The event, initially designated G184098 and later given the name GW150914, is described in detail elsewhere. By prior arrangement, preliminary estimates of the time, significance, and sky location of the event were shared with 63 teams of observers covering radio, optical, near-infrared, X-ray, and gamma-ray wavelengths with ground- and space-based facilities. In this Letter we describe the low-latency analysis of the GW data and present the sky localization of the first observed compact binary merger. We summarize the follow-up observations reported by 25 teams via private Gamma-ray Coordinates Network circulars, giving an overview of the participating facilities, the GW sky localization coverage, the timeline, and depth of the observations. As this event turned out to be a binary black hole merger, there is little expectation of a detectable electromagnetic (EM) signature. Nevertheless, this first broadband campaign to search for a counterpart of an Advanced LIGO source represents a milestone and highlights the broad capabilities of the transient astronomy community and the observing strategies that have been developed to pursue neutron star binary merger events. Detailed investigations of the EM data and results of the EM follow-up campaign are being disseminated in papers by the individual teams. </p

FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media

With increasing use of proteins in many different applications, ranging from phramaceuticals to biosensors and biomaterials, there has emerged a need for protein structural characterisation in diverse environments. In many cases it is not sufficient to just have the three-dimensional structure of a protein in H2O or in the crystalline state. Often information on the structural properties of a protein is required in the presence of organic solvents, detergent micelles, phospholipid membranes and so on. Fourier transform infrared spectroscopy (FTIR) has been identified as one of the few techniques that can be applied for structural characterisation of proteins in such environments. Here we discuss how this technique is being used to obtain information on protein structure and stability in both aqueous and non-aqueous media. Examples are drawn from our studies of water soluble proteins and membrane proteins

Fourier transform infrared spectroscopy suggests unfolding of loop structures precedes complete unfolding of pig citrate synthase

Pig citrate synthase (PCS) can be used as a model enzyme to gain some insight into the structural basis of protein thermostability. The thermal unfolding characteristics of the specific secondary structure elements within PCS were monitored in detail by following changes in its amide I band components. The result of our study indicates that PCS undergoes irreversible thermal denaturation. Detailed analysis reveals that the different secondary structures display a multistep transition with a major and a minor transition at different temperatures and a very small initial transition at the same temperature (30degreesC). A plot of temperature-induced changes in H-1-H-2 exchange, the decrease in the absorbance of the a-helical structures, and the increase in the absorbance of aggregated structures all have in common a multistep transition, the minor one centered at 45degreesC and the major one around 59degreesC. In contrast, a band that is tentatively assigned to loop structures displays these same minor and major transitions but at lower temperatures (39 and 52degreesC, respectively). The transition, which occurs at 39-45degreesC, is not associated with the appearance of aggregated structures. This transition may reflect a change in the tertiary structure of the protein. However, the final transition, which occurs at a higher temperature (52-59degreesC), reflects unfolding and aggregation of the polypeptide chains. The Fourier transform infrared (FTIR) analysis suggests that PCS has a thermolabile region that unfolds first, some 7degreesC below the main unfolding of the protein. We propose that this reflects the unfolding of the highly flexible loop segments, which in turn triggers the unfolding of the predominantly helical core structure of PCS. (C) 2003 Wiley Periodicals, Inc

Vibrational spectroscopy in diagnosis and screening

In recent years there has been a tremendous growth in the use of vibrational spectroscopic methods for diagnosis and screening. These applications range from diagnosis of disease states in humans, such as cancer, to rapid identification and screening of microorganisms. The growth in such types of studies has been possible thanks to advances in instrumentation and associated computational and mathematical tools for data processing and analysis. This volume of Advances in Biomedical Spectroscopy contains chapters from leading experts who discuss the latest advances in the application of Fourie

Development of biotechnology education in Turkey

For sometime Turkish scientists have been actively involved in biotechnology related research. However, biotechnology education in Turkey is a relatively recent phenomenon. The subject has not been addressed at the undergraduate level in a serious way until recently, This is evident from the lack of undergraduate degree programmes in biotechnology at Turkish Universities. The Turkish scientific establishment is very much aware of the importance of biotechnology and has identified this subject as one of the priority areas. The Universities are taking positive steps towards enhancing Biotechnology education. This article focuses on the emergence, as well as the problems and prospects of Biotechnology education in Turkey. (C) 2000 IUBMB. Published by Elsevier Science Ltd. All rights reserved

POTENTIAL OF C-13 AND N-15 LABELING FOR STUDYING PROTEIN-PROTEIN INTERACTIONS USING FOURIER-TRANSFORM INFRARED-SPECTROSCOPY

In this study, we examine the interaction between two bacterial proteins, namely HPr and IIA(mtl) of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system, using FTIR spectroscopy. In an interaction involving a 1:1 molar ratio of these two proteins, when they are unlabeled, the overlap of absorbance of the amide I band arising from the peptide group vibrations of the two proteins is such that it is not possible to determine the contribution which each protein makes to the absorbance. Uniform N-15 labeling has little effect on the frequency of the amide I band although there is a significant shift of the amide II band. However, we show that uniform (90%) C-13 labeling produces a large shift of bands associated with the carbonyl moiety, especially the amide I band. This opens up windows in different regions of the infrared spectrum. Thus, when the same mixture of the two bacterial proteins is made where one of the proteins is uniformly C-13-labeled (in our case HPr), the amide I maxima of this protein shifts by approximately 45 cm-1 toward lower frequency and reveals the previously overlapped amide I band of the unlabeled IIA(mtl). This application of C-13 labeling shows the potential of studying protein-protein interactions using FTIR spectroscopy. With thoughtful selection of systems and labeling strategies, numerous studies with proteins should be possible. These could include, among others, enzyme-substrate and protein-ligand interactions

POTENTIAL OF C-13 AND N-15 LABELING FOR STUDYING PROTEIN-PROTEIN INTERACTIONS USING FOURIER-TRANSFORM INFRARED-SPECTROSCOPY

In this study, we examine the interaction between two bacterial proteins, namely HPr and IIA(mtl) of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system, using FTIR spectroscopy. In an interaction involving a 1:1 molar ratio of these two proteins, when they are unlabeled, the overlap of absorbance of the amide I band arising from the peptide group vibrations of the two proteins is such that it is not possible to determine the contribution which each protein makes to the absorbance. Uniform N-15 labeling has little effect on the frequency of the amide I band although there is a significant shift of the amide II band. However, we show that uniform (90%) C-13 labeling produces a large shift of bands associated with the carbonyl moiety, especially the amide I band. This opens up windows in different regions of the infrared spectrum. Thus, when the same mixture of the two bacterial proteins is made where one of the proteins is uniformly C-13-labeled (in our case HPr), the amide I maxima of this protein shifts by approximately 45 cm-1 toward lower frequency and reveals the previously overlapped amide I band of the unlabeled IIA(mtl). This application of C-13 labeling shows the potential of studying protein-protein interactions using FTIR spectroscopy. With thoughtful selection of systems and labeling strategies, numerous studies with proteins should be possible. These could include, among others, enzyme-substrate and protein-ligand interactions