DIVERSIFIKASI EKSPOR NON MIGAS INDONESIA KE PASAR NON TRADISIONAL

Abstrak Penelitian ini bertujuan untuk menganalisis diversifikasi ekspor non migas Indonesia ke pasar non tradisional. Metode penelitian yang digunakan adalah analisis statistik deskriptif dengan pendekatan pengelompokan (clustering), Structural Match Index dan Demand Index, serta regresi data panel. Hasil penelitian menunjukkan bahwa negara yang diidentifikasikan sebagai negara non tradisional potensial adalah Brazil, Pantai Gading, Mesir, Georgia, Jamaica, Kazakhstan, Kuwait, Myanmar, Nigeria, Norway, Oman, Pakistan, Russian Federation, Trinidad and Tobago, Turkey, United Arab Emirates, dan Uruguay. Hasil regresi data panel menunjukkan bahwa Random Effect Model merupakan model yang terbaik untuk menjelaskan faktor-faktor yang memengaruhi ekspor non migas Indonesia ke negara non tradisional. Hasil regresi menunjukkan bahwa GDP riil negara tujuan, populasi negara tujuan, nilai tukar riil, FDI dan kualitas pelabuhan Indonesia berpengaruh signifikan secara statistik terhadap ekspor non migas Indonesia ke negara non tradisional potensial tersebut. Beberapa rekomendasi kebijakan yang perlu dilakukan untuk meningkatkan ekspor non migas ke negara tujuan non tradisional diantaranya perlu dilakukan intelejen pasar mengenai kebutuhan dan selera dari masing-masing negara non tradisional atas produk Indonesia, peningkatan kualitas pelabuhan Indonesia dan kebijakan tambahan yang memberikan insentif untuk menarik Foreign Direct Investment ke Indonesia. Kata Kunci: Diversifikasi Ekspor, Demand Index, Non traditional, Random Effect Model, Structural Match Index Abstract This study aims to analyze the diversification of Indonesia's non-oil and gas exports to non-traditional markets. The research method used is descriptive statistical analysis with a clustering approach, Structural Match Index and demand index, and panel data regression. The results showed that countries identified as potential non-traditional countries were Brazil, Ivory Coast, Egypt, Georgia, Jamaica, Kazakhstan, Kuwait, Myanmar, Nigeria, Norway, Oman, Pakistan, Russian Federation, Trinidad and Tobago, Turkey, United Arab Emirates, and Uruguay. The panel data regression results show that the random effect model is the best model to explain the factors that influence Indonesia's non-oil exports to non-traditional countries. The results show that the real GDP of the destination country, the population of the destination country, the real exchange rate, FDI and the quality of Indonesia's ports have a statistically significant effect on Indonesia's non-oil exports to these potential non-traditional countries. Then, in this study there are several policy recommendations that need to be done to increase non-oil and gas exports to non-traditional destination countries including market intelligence regarding the needs and tastes of each non-traditional country for Indonesian products, improving the quality of Indonesian ports and additional policies that provide incentives to attract Foreign Direct Investment to Indonesia. Keywords: Export Diversification, Demand Index, Non-traditional, Random Effect Model, Structural Match Index JEL Classifications: F13, F15, F18

BioMetAll: Identifying Metal-Binding Sites in Proteins from Backbone Preorganization

<div><div><div><p>With a large amount of research dedicated to decoding how metallic species bind to protein, in silico methods are interesting allies for experimental procedures. To date, computational predictors mostly work by identifying the best possible sequence or structural match of the target protein with metal binding templates. These approaches are fundamentally focused on the first coordination sphere of the metal. Here, we present the BioMetAll predictor that is based on a different postulate: the formation of a potential metal-binding site is related to the geometric organization of the protein backbone. We first report the set of convenient geometric descriptors of the backbone needed for the algorithm and their parametrization from a statistical analysis. Then, the successful benchmark of BioMetAll on a set of more than 50 metal-binding X-Ray structures is presented. Because BioMetAll allows structural predictions regardless of the exact geometry of the side chains, it appears extremely valuable for systems which structures (either experimental or theoretical) are not optimal for metal binding sites. We report here its application on three different challenging cases i) the modulation of metal-binding sites during conformational transition in human serum albumin, ii) the identification of possible routes of metal migration in hemocyanins, and iii) the prediction of mutations to generate convenient metal-binding sites for de novo biocatalysts. This study shows that BioMetAll offers a versatile platform for numerous fields of research at the interface between inorganic chemistry and biology, and allows to highlight the role of the preorganization of the protein backbone as a marker for metal binding.</p></div></div></div>

BioMetAll: Identifying Metal-Binding Sites in Proteins from Backbone Preorganization

<div><div><div><p>With a large amount of research dedicated to decoding how metallic species bind to protein, in silico methods are interesting allies for experimental procedures. To date, computational predictors mostly work by identifying the best possible sequence or structural match of the target protein with metal binding templates. These approaches are fundamentally focused on the first coordination sphere of the metal. Here, we present the BioMetAll predictor that is based on a different postulate: the formation of a potential metal-binding site is related to the geometric organization of the protein backbone. We first report the set of convenient geometric descriptors of the backbone needed for the algorithm and their parametrization from a statistical analysis. Then, the successful benchmark of BioMetAll on a set of more than 50 metal-binding X-Ray structures is presented. Because BioMetAll allows structural predictions regardless of the exact geometry of the side chains, it appears extremely valuable for systems which structures (either experimental or theoretical) are not optimal for metal binding sites. We report here its application on three different challenging cases i) the modulation of metal-binding sites during conformational transition in human serum albumin, ii) the identification of possible routes of metal migration in hemocyanins, and iii) the prediction of mutations to generate convenient metal-binding sites for de novo biocatalysts. This study shows that BioMetAll offers a versatile platform for numerous fields of research at the interface between inorganic chemistry and biology, and allows to highlight the role of the preorganization of the protein backbone as a marker for metal binding.</p></div></div></div>

Simulating preferential sorption of tartrate on prismatic calcite surfaces

Calculated binding energies of favorable adsorption configurations emphasize the importance of surface charge/energetics, structural match and water layers in mineral–organic interactions.

On the Difference in Quality between Current Heuristic and Optimal Solutions to the Protein Structure Alignment Problem

The importance of pairwise protein structural comparison in biomedical research is fueling the search for algorithms capable of finding more accurate structural match of two input proteins in a timely manner. In recent years, we have witnessed rapid advances in the development of methods for approximate and optimal solutions to the protein structure matching problem. Albeit slow, these methods can be extremely useful in assessing the accuracy of more efficient, heuristic algorithms. We utilize a recently developed approximation algorithm for protein structure matching to demonstrate that a deep search of the protein superposition space leads to increased alignment accuracy with respect to many well-established measures of alignment quality. The results of our study suggest that a large and important part of the protein superposition space remains unexplored by current techniques for protein structure alignment.

INTERACTION BETWEEN Li+ CATION WITH CROWN ETHERS OF Bz15C5, DBz16C5 AND DBz18C6: MOLECULAR MODELING BASE ON MNDO/d SEMIEMPIRICAL METHOD

The aim of this research is to find information about the substituent effect to the structure of crown ether benzo-15-crown-5 (Bz15C5), dibenzo-16-crown-5 (DBz16C5) and dibenzo-18-crown-6 (DBz18C6), and also crown ether selectivity to coordinate a Li+ metal cation. The presence of substituent could change the conformations flexibility of crown ether during interact with metal cation. In this research semi empirical MNDO/d method was used for calculations. Firstly, geometry optimization was conducted to crown ethers structure using MNDO/d methods. The next steps were running the geometry optimization of complexes between cation Li+ with crown ethers. Data were produced from these calculation are the parameter of crown ether structures, structures of the complexes, and the binding energy of the cation-crown ethers. The presence of electron-withdrawing substituents decreased the binding energy while that of electron-donating one increase the binding energy (value of ΔE more negative). The substituents which are increase the degree of symmetry of the cation-crown ether complexes could give the increase of crown ether selectivity to bind the cation. Selectivity of crown ether to bind the cation depends on the structural match between ionic radii of crown ether cavity (the ion-cavity size concept). Bz15C5 what has higher selectivity to bind Li+ than DBz16C5 and DBz18C6. Keywords: selectivity, crown ether, MNDO/d.

STRUCTURAL BASIS OF ANTIFREEZE PROTEIN ACTION

Antifreeze Proteins (AFPs) modify the growth rates and orientations of ice crystal facets through attainment of the best structural match. The insect-type AFPs have ice binding surfaces (IBS) with regularly spaced binding intervals in two directions that engage the primary ice surfaces and reduce their growth rates preferentially. The primary ice surfaces are kinetically stable and have fixed orientations, since they are strongly bonded in two directions. The fish-type AFPs have one-dimensional helical and irregular globular IBSs that are either linearly extended with regular ice binding intervals, or have ice binding sites lacking spacing regularity. They adjust the orientations of the secondary ice surfaces, that have indeterminate face indices since they are strongly bonded in only one direction. The fish-type AFPs stabilize secondary ice surfaces and adjust their orientations by mimicking strong bonding directions, that are not present in the ice structure. The theory agrees with experimental observation and explains hitherto unexplained phenomena. The observed broad variation in prismatic and, more importantly, pyramidal ice crystallites produced in the presence of fish-type AFPs is explained, since these faces are secondary. The observed crystals triggered by most insect-type AFPs are disk shaped, because they consist of primary ice surfaces. The allegedly exceptional ice pyramids triggered by the insect-type TmAFP are the primary ice pyramid with fixed indices, and entirely different from the pyramids of the fish-type AFPs.

NEW UNDERSTANDINGS FOR THREE-DIMENSIONAL NUCLEATION (I)

The generic heterogeneous effect of foreign particles on 3D nucleation was examined both theoretically and experimentally. It shows that the nucleation observed under normal conditions includes a sequence of progressive heterogeneous processes, characterized by different interfacial correlation function f(m, x) s . At low supersaturations, nucleation will be controlled by the process with a small interfacial correlation function f(m, x), which results from a strong interaction and good structural match between the foreign bodies and the crystallizing phase. At high supersaturations, nucleation on foreign particles having a weak interaction and poor structural match with the crystallizing phase (f(m, x)→1) will govern the kinetics. This frequently leads to the false identification of homogeneous nucleation. Genuine homogeneous nucleation, which is the up-limit of heterogeneous nucleation, may not be easily achievable under gravity. In order to check these results, the prediction is confronted with nucleation experiments of some crystals. The results are in excellent agreement with the theory. Apart from this, the implications for epitaxial growth have also been discussed. In order to grow crystals epitaxially, the supersaturation should be kept at a low level, despite a good structural match between the crystal and substrate.