Petua Menjadi Pelajar Cemerlang Menurut Al-Quran

Petua Menjadi Pelajar Cemerlang Menurut Al-Quran

BULAN SYAABAN ^_^

Alhamdulillah., tnpe kite sedar, telah sampai bulan Syaaban...,

Sungguh bersyukur kepada Allah Yang Maha Esa.,

Kerana kite msih bernafas di ats muka bumi -Nya..,

Smoge dgn kdtgn buln yg mulia ini.,

Kite dpt mnyediakn diri kte utk brtemu Allah...

“Ya Allah berkatilah kami pada bulan Rejab dan Syaaban dan sampaikanlah kami ke bulan Ramadhan”

..Makbulkanlah doa kami Ya Allah. AMIN..

Abdullah b Yusuf menyampaikan kepada kami, dari Malik, dari Abi An-Nadr, dari Abi Salamah, dari Aisyah ra. dia berkata (bermaksud), “Adalah Rasulullah saw berpuasa sehingga kami mengatakan dia tidak berbuka. Dia saw berbuka sehingga kami mengatakan dia tidak berpuasa. Aku tidak pernah melihat Nabi saw berpuasa penuh satu bulan melainkan (dalam bulan) Ramadan. Aku tidak pernah melihat dia saw berpuasa lebih banyak selain dari bulan Syaaban” (Hadis Sahih No. 1969 riwayat Imam Al-Bukhari)

Antara kelebihn bulan Syaaban :  

1. Setiap amalan kebajikan akan digandakan oleh Allah dengan 700 kali ganda
2. Allah akan menurunkan rahmatNya serta memberikan pengampunan umum kepada hambanya
3. Sesiapa yang berpuasa 3 hari di awal, pertengahan dan akhirnya maka Allah akan menuliskan baginya pahala 70 orang nabi-nabi, pahala beribadat selama 70 tahun dan jika ia meninggal pada tahun itu maka ia akan mendapat pahala mati syahid
4. Kelebihan malam nifsu Syaaban pula ialah sesiapa yang bangun mendirikan solat sunat dan menghidupkan malam itu dengan banyak berdoa, berzikir, berselawat, bertasbih, membaca Al Quran dan sebagainya maka Allah akan membukakan untuknya 300 pintu rahmat disamping doanya tidak akan ditolak
5. Orang-orang yang tidak diampunkan oleh Allah pada malam nifsu Syaaban ialah mereka yang menyekutukan Allah dengan sesuatu, tukang sihir, tukang nujum, mereka yang suka bermusuhan, peminum arak, penzina, pemakan riba, derhaka terhadap ibu bapa, pembuat fitnah dan mereka yang memutuskan tali silaturrahim.

wallahua'lam....=)))

DI MANAKAH CANTIKNYA SEORANG WANITA..=))

Mungkin pada sepasang matanya yang hening yang selalu menjeling tajam atau yang kadang kala malu-malu memberikan kerlingan manja.

Boleh jadi pada bibirnya yang tak jemu-jemu menyerlahkan senyuman manis, atau yang sekali-sekala memberikan kucupan mesra di dahi umi juga, ayah, suami dan pipi munggil anak-anak.

Atau mungkin juga pada hilai tawanya yang gemersik dan suara manjanya yang boleh melembut sekaligus melembutkan perasaan.

Sejuta perkataan belum cukup untuk menceritakan kecantikan perempuan. Sejuta malah berjuta-juta kali ganda perkataan pun masih belum cukup untuk mendefinisikan tentang keindahan perempuan. 

Kitalah perempuan itu. Panjatkan kesyukuran kehadrat Tuhan kerana menjadikan kita perempuan dan memberikan keindahan-keindahan itu.

Namun, betapa pun dijaga, dipelihara, dibelai dan ditatap di hadapan cermin saban waktu, tiba masanya segalanya akan pergi jua. Wajah akan suram, mata akan kelam.

Satu sahaja yang tidak akan dimamah usia, sifat keperempuanan yang dipupuk dengan iman dan ibadah.

Anda ingin lebih cantik dan menarik?

# Jadikanlah Ghadhdul Bashar (menundukkan pandangan) sebagai "hiasan mata" anda, nescaya akan semakin bening dan jernih.

# Oleskan "lipstik kejujuran" pada bibir anda, nescaya akan semakin manis.

# Gunakanlah "pemerah pipi" anda dengan kosmetik yang terbuat dari rasa malu yang dibuat dari salon Iman.

# Pakailah "sabun istighfar" yang menghilangkan semua dosa dan kesalahan yang anda lakukan.

# Rawatlah rambut anda dengan "selendang islami" yang akan menghilangkan kelemumur pandangan lelaki.

# Hiasilah kedua tangan anda dengan gelang tawadhu' dan jari-jari anda dengan cincin ukhuwwah.

# Sebaik-baiknya kalung anda adalah kalung "kesucian."

# Bedaklah wajah anda dengan "air wudhu."     

RAHSIA KHUSYUK DALAM SOLAT

Diriwayatkan pada zaman dulu ada seorang ahli ibadat bernama Isam bin Yusuf yang terkenal warak serta sentiasa khusyuk dalam mengerjakan solat. Bagaimanapun, sebagai manusia, Isam selalu tertanya mengenai ibadat yang dilakukan berikutan khuatir ia tidak khusyuk menyebabkan dia sering bertanya kepada ahli ibadat lain bagi memperbaiki dirinya.

Namun, pada suatu hari, Isam menghampiri seorang abid bernama Hatim Al-Assam lalu bertanya: "wahai Aba Abdurrhaman,bagaimanakah caranya tuan mengerjakan solat?" Lalu dijawab Hatim: "Apabila masuk waktu solat, aku berwuduk zahir dan batin."

Kerana ingin mengetahui lebih lanjut, Isam bertanya: "Bagaimana pula caranya wuduk zahir dan batin itu?" Dijawab oleh Hatim: "Wuduk zahir adalah sama seperti kita membasuh anggota dengan menggunakan air tetapi wuduk batin adalah dengan membasuh seluruh anggota badan menerusi tujuh perkara iaitu bertaubat, menyesali dosa yang dilakukan, tidak terlalu mencintai dunia, tidak berharap pada pujian, meninggalkan sifat bangga, meninggalkan sifat khianat dan menipu, serta meninggalkan sifat dengki."

Seterusnya,Hatim berkata: "Apabila sesudah aku berwuduk zahir dan batin, lalu aku terus ke masjid, aku kemaskan anggota tubuhku dan terus menghadap kiblat dengan perasaan aku menghadap Allah SWT, syurga di sebelah kananku, neraka di sebelah kiriku, dan malaikat maut di belakangku. Sesudah itu, aku bayangkan berdiri di atas titian Siratul Mustaqim dengan menganggap solatku ini adalah solat yang terakhir, lalu aku berniat dan bertakbir dengan sebaik-baiknya. Ketika di dalam solat, aku menghayati bacaan dan doa yang diucapkan, aku pastikan aku memahami maksudnya sebelum aku rukuk dan sujud dengan penuh tawaduk, lantas aku bertasyadud dengan sepenuh keikhlasan hati. Beginilah caranya aku bersolat selama 30 tahun," katanya.

Apabila mendengar penerangan itu,menangislah Isam kerana membayangkan ibadat dilakukannya kurang baik berbanding Hatim. Menerusi kisah ini, dapat disimpulkan bahawa bagi mencapai solat yang khusyuk, seseorang itu bukan saja perlu meninggalkan setiap sifat buruk di dalam diri, malah perlu memahami maksud bacaan yang diucapkan.. 

Selamat beramal >_<

SCATTER PLOT IN EXCEL

Objectives

• Enter and format data in an Excel spreadsheet in a form appropriate for graphing
• Create a scatter plot from spreadsheet data
• Insert a linear regression line (trendline) into the scatter plot
• Use the slope/intercept formula for the regression line to calculate a x value for a known y value
• Explore curve fitting to scatterplot data
• Create a connected point (line) graph
• Place a reference line in a graph

Below are some examples:

SMILES

SMILES (Simplified Molecular Input Line Entry System) is a line notation (a typographical method using printable characters) for entering and representing molecules and reactions. SMILES contains the same information as might be found in an extended connection table. The primary reason SMILES is more useful than a connection table is that it is a linguistic construct, rather than a computer data structure. SMILES is a true language, albeit with a simple vocabulary (atom and bond symbols) and only a few grammar rules. SMILES representations of structure can in turn be used as "words" in the vocabulary of other languages designed for storage of chemical information (information about chemicals) and chemical intelligence (information about chemistry).

These properties open many doors to the chemical information programmer. Examples of uses for SMILES are:

• Keys for database access
• Mechanism for researchers to exchange chemical information
• Entry system for chemical data
• Part of languages for artificial intelligence or expert systems in chemistry

PROTEIN DATA BANK

The Protein Data Bank (PDB) is a repository for the 3-D structural data of large biological molecules, such as proteins and nucleic acids. (See also crystallographic database). The data, typically obtained by X-ray crystallography or NMR spectroscopybiologists and biochemists from around the world, are freely accessible on the Internet via the websites of its member organisations (PDBe, PDBj, and RCSB). The PDB is overseen by an organization called the Worldwide Protein Data Bank, 

The PDB is a key resource in areas of structural biology, such as structural genomics. Most major scientific journals, and some funding agencies, such as the NIH in the USA, now require scientists to submit their structure data to the PDB. If the contents of the PDB are thought of as primary data, then there are hundreds of derived (i.e., secondary) databases that categorize the data differently. For example, both SCOP and CATH categorize structures according to type of structure and assumed evolutionary relations; GO categorize structures based on genes.

The PDB originated as a grassroots effort.In 1971, Walter Hamilton of the Brookhaven National Laboratory agreed to set up the data bank at Brookhaven. Upon Hamilton's death in 1973, Tom Koeztle took over direction of the PDB. In January 1994, Joel Sussman was appointed head of the PDB. In October 1998,^[2] the PDB was transferred to the Research Collaboratory for Structural Bioinformatics (RCSB); the transfer was completed in June 1999. The new director was Helen M. Berman of Rutgers University (one of the member institutions of the RCSB).^[3] In 2003, with the formation of the wwPDB, the PDB became an international organization. The founding members are PDBe (Europe), RCSB(USA), and PDBj (Japan). The BMRB joined in 2006. Each of the four members of wwPDB can act as deposition, data processing and distribution centers for PDB data. The data processing refers to the fact that wwPDB staff review and annotates each submitted entry. The data are then automatically checked for plausibility. (The source code for this validation software has been made available to the public at no charge.

The file format initially used by the PDB was called the PDB file format. This original format was restricted by the width of computer punch cards to 80 characters per line. Around 1996, the "macromolecular Crystallographic Information file" format, mmCIF, started to be phased in. An XML version of this format, called PDBML, was described in 2005.The structure files can be downloaded in any of these three formats. In fact, individual files are easily downloaded into graphics packages using web addresses:

• For PDB format files, use, e.g., http://www.pdb.org/pdb/files/4hhb.pdb.gz or http://pdbe.org/download/4hhb
• For PDBML (XML) files, use, e.g., http://www.pdb.org/pdb/files/4hhb.xml.gz or http://pdbe.org/pdbml/4hhb

The "4hhb" is the PDB identifier. Each structure published in PDB receives a four-character alphanumeric identifier, its PDB ID. (This cannot be used as an identifier for biomolecules, because often several structures for the same molecule—in different environments or conformations—are contained in PDB with different PDB IDs.)

HtrA 
H198P/T167V DOUBLE MUTANT OF DEGS-DELTAPDZ PROTEASE

Primary Citation Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution. Sohn, J.,   Grant, R.A.,   Sauer, R.T. Journal: (2010) J.Biol.Chem. 285: 34039-34047 PubMed: 20739286   PubMedCentral: PMC2962503   DOI: 10.1074/jbc.M110.135541   Search Related Articles in PubMed   PubMed Abstract: DegS is a periplasmic Escherichia coli protease, which functions as a trimer to catalyze the initial rate-limiting  step in a proteolytic cascade that ultimately activates transcription of stress response genes in the cytoplasm.  Each DegS subunit consists of a proteas. DegS is a periplasmic Escherichia coli protease, which functions as a trimer to catalyze the initial rate-limiting step in a proteolytic cascade that ultimately activates transcription of stress response genes in the cytoplasm. Each DegS subunit consists of a protease domain and a PDZ domain. During protein folding stress, DegS is allosterically activated by peptides exposed in misfolded outer membrane porins, which bind to the PDZ domain and stabilize the active protease. It is not known whether allostery is conferred by the PDZ domains or is an intrinsic feature of the trimeric protease domain. Here, we demonstrate that free DegS(?PDZ) equilibrates between active and inactive trimers with the latter species predominating. Substrate binding stabilizes active DegS(?PDZ) in a positively cooperative fashion. Mutations can also stabilize active DegS(?PDZ) and produce an enzyme that displays hyperbolic kinetics and degrades substrate with a maximal velocity within error of that for fully activated, intact DegS. Crystal structures of multiple DegS(?PDZ) variants, in functional and non-functional conformations, support a two-state model in which allosteric switching is mediated by changes in specific elements of tertiary structure in the context of an invariant trimeric base. Overall, our results indicate that protein substrates must bind sufficiently tightly and specifically to the functional conformation of DegS(?PDZ) to assist their own degradation. Thus, substrate binding alone may have regulated the activities of ancestral DegS trimers with subsequent fusion of the protease domain to a PDZ domain, resulting in ligand-mediated regulation. Keywords: Allosteric Site, Bacterial Proteins, Crystallography, X-Ray, Dimerization, Escherichia coli, Escherichia coli Proteins, Gene Expression Regulation, Bacterial, Hydrogen Bonding, Kinetics, Mutation, Protein Binding, Protein Folding, Protein Structure, Tertiary Related Structures: Primary Citation of:  3LGI   3LGT   3LGU   3LGV   3LGW   3LGY   3LH1   3LH3       Organizational Affiliation: Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA. Click on abstract words and keywords to add them to the search box. [Hide Abstract] Molecule: Protease degS Polymer: 1 Type: polypeptide(L) Length: 241 Chains: A EC#: 3.4.21.-     Fragment: protease domain Classification: Hydrolase Structure Weight: 25847.40

LonA
CRYSTAL STRUCTURE OF BACILLUS SUBTILIS LON N-TEMINAL DOMAIN

Primary Citation

Crystal structures of Bacillus subtilis Lon protease.
Duman, R.E.,   Lowe, J.
Journal: (2010) J.Mol.Biol. 401: 653-670

PubMed: 20600124  
DOI: 10.1016/j.jmb.2010.06.030  
Search Related Articles in PubMed  

PubMed Abstract:

Lon ATP-dependent proteases are key components of the protein quality control systems of bacterial cells
and eukaryotic organelles. Eubacterial Lon proteases contain an N-terminal domain, 
an ATPase domain, and a protease domain, all in one polypeptide chain. The N-terminal domain.

Lon ATP-dependent proteases are key components of the protein quality control systems of bacterial cells and eukaryotic organelles. Eubacterial Lon proteases contain an N-terminal domain, an ATPase domain, and a protease domain, all in one polypeptide chain. The N-terminal domain is thought to be involved in substrate recognition, the ATPase domain in substrate unfolding and translocation into the protease chamber, and the protease domain in the hydrolysis of polypeptides into small peptide fragments. Like other AAA+ ATPases and self-compartmentalising proteases, Lon functions as an oligomeric complex, although the subunit stoichiometry is currently unclear. Here, we present crystal structures of truncated versions of Lon protease from Bacillus subtilis (BsLon), which reveal previously unknown architectural features of Lon complexes. Our analytical ultracentrifugation and electron microscopy show different oligomerisation of Lon proteases from two different bacterial species, Aquifex aeolicus and B. subtilis. The structure of BsLon-AP shows a hexameric complex consisting of a small part of the N-terminal domain, the ATPase, and protease domains. The structure shows the approximate arrangement of the three functional domains of Lon. It also reveals a resemblance between the architecture of Lon proteases and the bacterial proteasome-like protease HslUV. Our second structure, BsLon-N, represents the first 209 amino acids of the N-terminal domain of BsLon and consists of a globular domain, similar in structure to the E. coli Lon N-terminal domain, and an additional four-helix bundle, which is part of a predicted coiled-coil region. An unexpected dimeric interaction between BsLon-N monomers reveals the possibility that Lon complexes may be stabilised by coiled-coil interactions between neighbouring N-terminal domains. Together, BsLon-N and BsLon-AP are 36 amino acids short of offering a complete picture of a full-length Lon protease.

Keywords:
Bacillus subtilis, Bacterial Proteins, Crystallography, X-Ray, Microscopy, Electron, Models, Molecular, Protease La, Protein Conformation, Protein Multimerization, Protein Structure, Tertiary

Related Structures:
Primary Citation of:  3M65   3M6A      

Organizational Affiliation:
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.


Click on abstract words and keywords to add them to the search box.

[Hide Abstract]

• Molecular Description

  Classification:	Hydrolase
  Structure Weight:	48027.40

  Molecule:

  ATP-dependent protease La 1

  Polymer:

  1

  Type:

  polypeptide(L)

  Length:

  209

  Chains:

  A, B

  EC#:

  3.4.21.53

  Fragment:

  BsLon, N-terminal domain
  
  
  
  CipP

STRUCTURE OF CIpP FROM BACILLUS SUBTILIS IN MONOCLINIC CRYSTAL FORM

Primary Citation

Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism.
Lee, B.-G.,   Park, E.Y.,   Lee, K.-E.,   Jeon, H.,   Sung, K.H.,   Paulsen, H.,   Rubsamen-Schaeff, H.,   Brotz-Oesterhelt, H.,   Song, H.K.
Journal: (2010) Nat.Struct.Mol.Biol. 17: 471-478

PubMed: 20305655  
DOI: 10.1038/nsmb.1787  
Search Related Articles in PubMed  

PubMed Abstract:

Clp-family proteins are prototypes for studying the mechanism of ATP-dependent proteases because the proteolytic activity of the ClpP core is tightly regulated by activating Clp-ATPases. Nonetheless, the proteolytic activation mechanism has remained elusive because of the lack of a complex.

Clp-family proteins are prototypes for studying the mechanism of ATP-dependent proteases because the proteolytic activity of the ClpP core is tightly regulated by activating Clp-ATPases. Nonetheless, the proteolytic activation mechanism has remained elusive because of the lack of a complex structure. Acyldepsipeptides (ADEPs), a recently discovered class of antibiotics, activate and disregulate ClpP. Here we have elucidated the structural changes underlying the ClpP activation process by ADEPs. We present the structures of Bacillus subtilis ClpP alone and in complex with ADEP1 and ADEP2. The structures show the closed-to-open-gate transition of the ClpP N-terminal segments upon activation as well as conformational changes restricted to the upper portion of ClpP. The direction of the conformational movement and the hydrophobic clustering that stabilizes the closed structure are markedly different from those of other ATP-dependent proteases, providing unprecedented insights into the activation of ClpP.

Keywords:
Anti-Bacterial Agents, Bacillus subtilis, Endopeptidase Clp, Escherichia coli Proteins, Peptides, Protein Conformation

Related Structures:
Primary Citation of:  3KTG   3KTH   3KTI   3KTJ   3KTK      

Organizational Affiliation:
School of Life Sciences and Biotechnology, Korea University, Seoul, Korea.


Click on abstract words and keywords to add them to the search box.

[Hide Abstract]

• Molecular Description

  
  

  
  

  Classification:	Hydrolase
  Structure Weight:	154303.80

  Molecule:	ATP-dependent Clp protease proteolytic subunit
  Polymer:	1	Type:	polypeptide(L)	Length:	199
  Chains:	A, B, C, D, E, F, G
  EC#:	3.4.21.92
  Mutation:	T193L,D195H,K196H,K19