Identifikasi Karakter Siswa Menggunakan Metode K-Means (Studi Kasus Sdn 156 Pekanbaru)

Good character education can have a characteristic impact on students. each student has a different character. Various ways done by the school in character education based on kemendiknas, including State Elementary School 156 Pekanbaru. Problems that arise in the field is there is no method that can determine the character of the students so that the school's special teachers can not understand precisely the characters in the students. The lack of understanding of the character of the students makes the vision of the school mission has not been seen so that character education in SDN 156 Pekanbaru has not been right target. Therefore, it needs to be done grouping student character in SDN 156 Pekanbaru with the aim of school know character owned by students in school. The K-Means algorithm is used to classify the character of the students with the number of clusters as much as 2 using the six attributes of characters studied: Honest, disciplined, confident, caring, creative and responsible with 130 student data. The results of K-Means manual calculation with sample data 10 data from 130 data that is weak character (C1) amounted to 1 student and weak character of 9 students, this result is same with calculation executed by RapidMiner application. Test results with 130 data using RapidMiner resulted in the number of students with weak character 26 students with the average centroid (0.665) with caring and creative characters. While students who have strong character 104 students with average value of centroid (0.900) with honest character, discipline, confidence, and responsibility. The result of character grouping based on class cluster position in RapidMiner is grade 3 which has weak character (C1) 8 students from 35 students, grade 4 is 8 out of 24 students, 5th grade is 1 of 17 students and grade 6 is 9 of 46 students. While clusters with strong characters (C2) class 3 amounted to 27 students, grade 4 amounted to 24 students, class 5 amounted to 16 students, and grade 6 amounted to 37 students. From the results of this study is expected Strong characters can be developed by school continue to perform habits which involves the students so that the characters in the students can be seen while for the caring and creative characters so as not to be weak then the school always provide guidance to the students and give examples of good habits and activities that can be followed by students in school

Estrogen receptor transcription and transactivation: Basic aspects of estrogen action

Estrogen signaling has turned out to be much more complex and exciting than previously thought; the paradigm shift in our understanding of estrogen action came in 1996, when the presence of a new estrogen receptor (ER), ERβ, was reported. An intricate interplay between the classical ERα and the novel ERβ is of paramount importance for the final biological effect of estrogen in different target cells

Structure and mechanism of the oestrogen receptor

We have determined the structures of the oestrogen receptor ligand-binding domain in complex with a range of ligands and with fragments of co-regulator proteins. These structures provide insights into the structural mechanisms underlying the receptor's complex pharmacological properties and how the conformation of the receptor modulates its ability to recruit co-regulators that are necessary for transcriptional activation

Structure of human factor VIIa and its implications for the triggering of blood coagulation

Factor VIIa (EC 3.4.21.21) is a trypsin-like serine protease that plays a key role in the blood coagulation cascade. On injury, factor VIIa forms a complex with its allosteric regulator, tissue factor, and initiates blood clotting. Although the structure of the binary complex has already been determined [Banner, D. W., D'Arcy, A., Chène, C., Winkler, F. K., Guha, A., Konigsberg, W. H., Nemerson, Y. and Kirchhofer, D. (1996) Nature (London) 380, 41-46], the conformational effects of cofactor binding to factor VIIa are not known in detail because of a lack of structural information on free factor VIIa. Here we report the structure of gamma-carboxyglutamic acid-domainless human coagulation factor VIIa at a resolution of 2.8 A. The molecule adopts an extended conformation within the crystal similar to that previously observed for the full-length protein in complex with tissue factor. Detailed comparison of free and tissue factor-bound factor VIIa reveals several structural differences. The binding mode of the active-site inhibitor D-Phe-Phe-Arg methyl ketone differs in the two structures, suggesting a role for the cofactor in substrate recognition. More importantly, a surface-exposed alpha-helix in the protease domain (residues 307-312), which is located at the cofactor recognition site, is distorted in the free form of factor VIIa. This subtle structural difference sheds light on the mechanism of the dramatic tissue factor-induced enhancement of factor VIIa activity

Structure of Fab hGR-2 F6, a competitive antagonist of the glucagon receptor.

The monoclonal antibody hGR-2 F6 has been raised against the human glucagon receptor and shown to act as a competitive antagonist. As a first step in the structural characterization of the receptor, the crystal structure of the Fab fragment from this antibody is reported at 2.1 A resolution. The hGR-2 F6 Fab crystallizes in the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 76.14, b = 133.74, c = 37.46 A. A model generated by homology modelling was used as an aid in the chain-tracing and the Fab fragment structure was subsequently refined (final R factor = 21.7%). The structure obtained exhibits the typical immunoglobulin fold. Complementarity-determining regions (CDRs) L1, L2, L3, H1 and H2 could be superposed onto standard canonical CDR loops. The H3 loop could be classified according to recently published rules regarding loop length, sequence and conformation. This loop is 14 residues long, with an approximate beta-hairpin geometry, which is distorted somewhat by the presence of two trans proline residues at the beginning of the loop. It is expected that this H3 loop will facilitate the design of synthetic probes for the glucagon receptor that may be used to investigate receptor activity

Lipid interactions of a ciliary membrane TRP channel: simulation and structural studies of Polycystin-2 (PC2)

Polycystin-2 (PC2) is a transient receptor potential (TRP) channel present in ciliary membranes of the kidney. PC2 shares a transmembrane fold with other TRP channels, in addition to an extracellular domain found in TRPP and TRPML channels. Using molecular dynamics (MD) simulations and cryoelectron microscopy we identify and characterize PIP2 and cholesterol interactions with PC2. PC2 is revealed to have a PIP binding site close to the equivalent vanilloid/lipid binding site in the TRPV1 channel. A 3.0-Å structure reveals a binding site for cholesterol on PC2. Cholesterol interactions with the channel at this site are characterized by MD simulations. The two classes of lipid binding sites are compared with sites observed in other TRPs and in Kv channels. These findings suggest PC2, in common with other ion channels, may be modulated by both PIPs and cholesterol, and position PC2 within an emerging model of the roles of lipids in the regulation and organization of ciliary membranes