Thursday, March 17, 2011

...........INSyaALLAH...........


Everytime you feel like you cannot go on
You feel so lost
That your so alone
All you is see is night
And darkness all around
You feel so helpless
You can’t see which way to go
Don’t despair and never loose hope
Cause Allah is always by your side

Insha Allah x3
Insya Allah you’ll find your way

Everytime you commit one more mistake
You feel you can’t repent
And that its way too late
Your’re so confused, wrong decisions you have made
Haunt your mind and your heart is full of shame

Don’t despair and never loose hope
Cause Allah is always by your side
Insha Allah x3
Insya Allah you’ll find your way
Insha Allah x3
Insya Allah you’ll find your way
Turn to Allah
He’s never far away
Put your trust in Him
Raise your hands and pray
OOO Ya Allah
Guide my steps don’t let me go astray
You’re the only one that showed me the way,
Showed me the way x2
Insha Allah x3
Insya Allah we’ll find the way

Friday, March 11, 2011

MataKu MilIKmu

Mataku Milikmu
www.iluvislam.com




" You have beautiful eyes "  

Perasaan cemas menghantui apabila mendengar sapaan berbaur 'flirting' nada melankolik daripada pemuda  Arab tersebut. Kulihat keadaan sekeliling sambil mempercepat langkah,  menoleh ke belakang setiap satu minit bagi memastikan diriku selamat dan tidak dikejar 
pemuda Arab itu tadi. Sungguh menakutkan.

Maha Suci Allah yang menciptakan segala sesuatu dengan penuh kesempurnaan, keindahan 
dan keajaiban. Teringat sebuah doa yang diajar Nabi untuk dibacakan apabila mendengar 
pujian daripada insan bergelar manusia. 


اللهم لا تؤاخذني بما يقولون ، واغفر لي مالا يعلمون واجعلني خيراً مما يظنون


" Ya Allah janganlah kamu mengapa-apakanku kerana apa yang disebut oleh mereka, dan ampunkankan daku berkaitan perkara yang mereka tidak ketahui (dan jadikanlah daku lebih baik dari apa yang mereka sangkakan. "
(Riwayat Abi Syaibah, no 35703, 7/242 ; At-Tarikh Al-Kabir, 2/58)


Bersyukur sungguh kerana Allah mengingatkan manusia untuk mengembalikan segala pujian dan kehormatan yang dikurniakan kepada manusia kembali kepada kuasa yang Maha Pemberi Kurnia iaitu Allah.  Pada hakikatnya segala-galanya yang diciptakan adalah milik Allah. Manusia tidak mempunyai daya dan kuasa untuk mencipta dan mengusai sesuatu perkara tanpa izinNya. 

Teringatku pada seloroh guruku ketika menerangkan hakikat ini. Katanya; 


" Manusia ni tak hebat langsung. Nak cipta tahi hidung sendiri pun tak boleh! "


Bahkan, anggota dan deria pada diri kita sendiri tertakluk kepada kekuasaannya.  


" Tahukah anda 'beautiful eyes' yang kita miliki sekarang terdiri daripada apa? "


Cuma air, lemak(lipid)gula (glucose)'receptor' yang diperbuat daripada 'protein'dan saraf yang diperbuat daripada serat. Semua bahan-bahan ini boleh didapati dari dapur rumah  masing-masing. Subhanallah.


" Bagaimana dengan bahan-bahan asas sebegini mampu menghasilkan fungsi yang menakjubkan? "


Daripada bahan yang sama juga mampu menghasilkan 'Beautiful eyes' yang 'bervariasi'warnanya. Terdapat manusia yang bermata  biru, coklat,  coklat pekat, coklat cair, kelabu, hijau dan lain-lain. Rahsia sebenarnya terletak pada struktur bernama 'iris' yang mempunyai ketebalan melanin yang berbeza. Contohnya, manusia yang mempunyai lapisan melanin yang nipis akan menzahirkan warna mata sebagai biru, iaitu warna 'salur darah vena' yang membawa 'deoxygenated blood' yang terdapat di belakang 'iris' . 

Kadang-kadang 'beautiful eyes' kita akan memberi gambaran yang salah terhadap sesuatu perspektif.  Pada hakikatnya ialah x, mata memberi gambaran y, dan kita pula membuat kesimpulan z.

Cuba perhatikan garisan biru dalam gambar berikut :



Nampak seperti senget bukan? Pada hakikatnya, garisan tersebut lurus! Tidak percaya? Anda boleh mengukurnya sendiri.
Terbukti melalui ujian mudah ini bahawa kita sendiri tidak mampu mengawal deria yang ada pada diri kita kerana segala-galanya adalah dibawah kawalan Allah.  Sebagai tanda kesyukuran dikurniakan 'beautiful eyes' dan nikmat yang pelbagai maka menjadi tanggungjawab kita untuk menzahirkan kesyukuran kita dengan mentawajuhkan atau menghalakan kiblat kehidupan kita dalam jalan yang diredhaiNya . 

Begitulah juga kehidupan ini, dihiasi dengan 'ilusi optik' yang mengelirukan lagi menyesatkan. Perkara yang jahiliyah dan buruk dilihat cantik dan mempesonakan manakala yang baik dan wangi dijauhi dan ditolak ke tepi.  Sepatutnya, semuanya perlu dilihat melalui kaca mata dan hati yang suci mengikut neraca Ilahi. Moga-moga hidup diberkati dan diredhai. Semoga 'beautiful eyes' kita ditemukan dengan Penciptanya di syurga nanti.
" Wahai Tuhan kami,tidaklah Engkau menjadikan benda-benda ini dengan sia-sia. Maha suci Engkau, maka peliharalah Kami dari azab neraka. "

Saturday, March 5, 2011

...to Late 4 Tears...

To Late For Tears
www.iluvislam.com
Submitted by: HJ Maniac
Editor: arisHa27

Death knocked on the bedroom door..

“Who is there?” The sleeping one cried.

“I’m angel Izrael, let me inside”. At once, the man began to shiver as one sweating in deadly fever.

He shouted to his wife, “Don’t let the Angel take my life. Oh Angel of Death, I’m not ready yet My family,depend on me. Give me a chance to go back and mend” 
The Angel knocked again..

“ Oh man, It’s your soul that I required, I come not with my own desire.” 
Bewildered, the man began to cry. “Oh Angel, I’m so afraid to die, Let me remain here as your slave, Don’t send me to the grave.” 

“Let me in, Oh man” the Angel said.

“Open the door, Get up from your bed. You can’t stop me from coming in, Angels can go through objects, thick and thin.” 
The man held a gun in his right hand and ready to defy the Angel’s stand.

“I’ll my gun towards your head. If you dare to come in, I’ll shoot you dead.” 

By now, the Angle was in the room, Saying, “Oh man,prepare for your doom, Foolish man – Angels never die. Put your gun and do not sigh. Why are you afraid? Tell me Oh man. To die according to Allah’s plan?” 

“Oh Angel, I bow my head in shame, I had no time to remember Allah’s name. From dawn till dusk, I made my wealth, Not even caring for my spiritual health. Allah’s commands I never obeyed, Nor five times a day I ever prayed. A Ramadhan came and A Ramadhan went, But no time had I repent. The Hajj was already obligatory upon me, But I would not part with my money. All charities I did ignore taking usury more and more. Sometimes I sipped my favourite wine, With flirting women I sat to dine. Oh Angel I appeal to you, Spare my life for a year or two. The laws of The Qur’an, I will obey, I’ll began Salat- this very day. My fast and Hajj I will complete, And keep away from self-conceit. I will refrain from usury, And give all my wealth to charity. Wine and unlawful women, I will detest, Allah’s oneness I will attest.” 


“We Angels do what Allah demands, We cannot go against His commands Death is ordained for everyone- father,mother,daughter and son. I’m afraid, this moment is your last, Now be reminded of your past. I do understand your fears But it is now too late for tears. You lived in this world, Two score or more, Your parents you did not obey, Hungry beggars, you turned away. Your two ill-mannered, female offspring In nightclubs, for livehood they sing. Instead of making more Muslims, You made your children non-Muslims. You ignored the Azan (call to prayer) Nor did you recite The Holy Qur’an. Breaking promises all your life, Backbiting friends and causing strife. From hoarded goods, Great profits you made, And your poor workers- You underpaid. Horses and cards were your leisure, Money-making was your pleasure You ate and ate, And grew more fat, With the very sick, you never sat. A little donation, you never gave That could a little baby save. You thought you’re clever and strong, But Oh man, You’ve done so many wrong. Paradise for you? I cannot tell The disbeliever will dwell in hell. There is no time for you to repent, I’ll take your soul for which I am sent.”




www.iluvislam.com

Sunday, February 6, 2011

...BeaUty...

I AM BEAUTIFUL AND YOU ARE TOO 
www.iluvislam.com
By: moslemische
Editor: salma ahsanan 

                      
I will say... "I am beautiful, you are beautiful, she is beautiful too, and they are all beautiful. We all will always look beautiful."

Then a person might ask me, "What makes you think that way? "Or the least, "Perasan...You look normal to me."

And what do you say? Isn't beauty is too subjective? Hard to identify and classify. Everyone is different."

Yeah I know...

"Beauty isn't just about the look. Beautiful person is the one with beautiful heartThe beauty is in the eyes of the beholder." 

"Look! She is beautiful! She is hot!. Put on some colors on your lips. You ain't look hot without make-ups, not beautiful..."

That is it. Enough! Different people with different definitions..Different people with different opinions..

Wait. If that so, how about those who were born to be "I am not beautiful" or "You are not beautiful?"  Do not worry. Do a plastic surgery!
Then waste my money? No. I do not want that. Even if I'm to be the richest person in the world.. I will never do that! Insha'Allah...

"But why not?"

Because you will end up being buried like other dead people do. Then after a while your beautiful skin, look, body will no longer be the same and will no longer look the same. You are no longer beautiful! Beautiful? Hot? Ugly? Hidious? It doesn't matter anymore. So what is up with all those plastic surgery and make-ups? They are not worthy. Not at all!

"So what's 'beauty' for you then?" 

Oh! Simple..."Natural pure-beauty..."

"How is that?"

My answer is: Be thankful for who you are, despite of how you looK, be thankful for what you have as Allah SWT has given you what is best for you, be thankful and stop comparing yourself with what other people have and feel enough with what you have will make you the richest person on earth..

Stop focusing on the physical (the look) and start perfecting your heart (manners). Thenyou will result in tranquility, trust me. Oh Muslims! We are all beautiful because we are Muslims. Beautiful by the way of Islam sees us. Beautiful by the way of Islam shapes us.Beautiful in a way Allah and his messenger wanted us to become to. 

So I will say...

"You and I are beautiful. No difference..."

Because you and I are the same,
Sharing a very common thing,
Sharing the same beauty of Islam,
Sharing Islam and that we are all Muslims.
Islam is beautiful. Therefore, we are all beautiful, insha'Allah...


     

 
source:www.iluvislam.com

Tuesday, January 25, 2011

EXCEL

.....Our assignment today is about linear regression and quadratic regeression.......


LINEAR REGRESSION

LINEAR REGRESSION  is an approach to modeling the relationship between a scalar variable y and one or more variables denoted X. In linear regression, models of the unknown parameters are estimated from the data using linear functions. Such models are called linear models. Most commonly, linear regression refers to a model in which the conditional mean of y given the value of X is an affine function of X. Less commonly, linear regression could refer to a model in which the median, or some other quantile of the conditional distribution of y given X is expressed as a linear function of X. Like all forms of regression analysis, linear regression focuses on the conditional probability distribution of y given X, rather than on the joint probability distribution of y and X, which is the domain of multivariate analysis.

QUADRATIC REGRESSION
 
QUADRATIC REGRESSION models are often used in economics areas such as utility function , forecasting, cost-befit analysis, etc. This JavaScript provides parabola regression model. This site also presents useful information about the characteristics of the fitted quadratic function.
Prior to using this JavaScript it is necessary to construct the scatter-diagram for your data.
If by visual inspection of the scatter-diagram, you cannot reject a "parabola shape", then you may use this JavaScript. Otherwise, visual inspection of the scatter-diagram enables you to determine what degree of polynomial regression models is the most appropriate for fitting to your data.










Tuesday, January 11, 2011

....SMILES....

INtroDucTION


The simplified molecular input line entry specification or SMILES is a specification for unambiguously describing the structure of chemical molecules using short ASCII strings. SMILES strings can be imported by most molecule editors for conversion back into two-dimensional drawings or three-dimensional models of the molecules.
The original SMILES specification was developed by Arthur Weininger and David Weininger in the late 1980s. It has since been modified and extended by others, most notably by Daylight Chemical Information Systems Inc.open standard called "OpenSMILES" was developed by the Blue Obelisk open-source chemistry community. Other 'linear' notations include the Wiswesser Line Notation (WLN), ROSDAL and SLN (Tripos Inc). In 2007, an
In July 2006, the IUPAC introduced the InChI as a standard for formula representation. SMILES is generally considered to have the advantage of being slightly more human-readable than InChI; it also has a wide base of software support with extensive theoretical (e.g., graph theory) backing.


SMILES - A Simplified Chemical Language

SMILES (Simplified Molecular Input Line Entry System) is a line notation (a typographical method using printable characters) for entering and representing molecules and reactions. Some examples are:
SMILESNameSMILESName
CC ethane [OH3+] hydronium ion
O=C=O carbon dioxide [2H]O[2H] deuterium oxide
C#N hydrogen cyanide [235U] uranium-235
CCN(CC)CC triethylamine F/C=C/F E-difluoroethene
CC(=O)O acetic acid F/C=C\F Z-difluoroethene
C1CCCCC1 cyclohexane N[C@@H](C)C(=O)O L-alanine
c1ccccc1 benzene N[C@H](C)C(=O)O D-alanine

Reaction SMILESName
[I-].[Na+].C=CCBr>>[Na+].[Br-].C=CCI displacement reaction
(C(=O)O).(OCC)>>(C(=O)OCC).(O) intermolecular esterification

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
 OUR asssignment today is about SMILES....Here it is...







Tuesday, January 4, 2011

....Protein Data Bank...

...InTroduction....

For simplicity, one can think of the PDB as a database of protein- and nucleic acid structures. However, it is important to keep in mind that the PDB entries are actually descriptions of structure determination experiments and their results. While such experiments usually aim at determining the structure of a protein or other macromolecule, the result of the experiment is actually just a model of the physical molecule.
The PDB was one of the first central repositories for biological data, preceding similar databases like Genbank for genomic sequences or Pubmed for biomedical literature. It was also one of the first examples where publication authors were required to submit experimental data to a central database before publication [5]. The PDB is now the single worldwide archive of structural data of biological macromolecules [3].

...HistoRY...

The PDB was initiated in 1971 by the Brookhaven National Laboratory in New York [2]. Some authors still refer to it as the Brookhaven Protein Data Bank even though it has not been associated with Brookhaven since 1999. Since this time the PDB has been maintained jointly by the Research Collaboratory for Structural Bioinformatics (RCSB), PDBe at the European Bioinformatics Institute (EBI), the PDBj in Japan and the BMRB (USA). These now form the Worldwide Protein Data Bank (wwPDB) organization, which was announced in 2003 [3]. The members of the wwPDB are maintaining and developing the PDB as the single and publicly available archive of macromolecular structural data.


...Ftsh PEptiDasE....



Authors: Han.S
Experiment:X-Ray Diffraction with resolution of 2.00A
Chain:A


FtsH is an ATP-dependent metalloprotease present as a hexameric heterocomplex in thylakoid membranes. Encoded in the Arabidopsis thaliana YELLOW VARIEGATED2 (VAR2) locus, FtsH2 is one isoform among major Type A (FtsH1/5) and Type B (FtsH2/8) isomers. Mutants lacking FtsH2 (var2) and FtsH5 (var1) are characterized by a typical leaf-variegated phenotype. The functional importance of the catalytic center (comprised by the zinc binding domain) in FtsH2 was assessed in this study by generating transgenic plants that ectopically expressed FtsH2(488), a proteolytically inactive version of FtsH2. The resulting amino acid substitution inhibited FtsH protease activity in vivo when introduced into Escherichia coli FtsH. By contrast, expression of FtsH2(488) rescued not only leaf variegation in var2 but also seedling lethality in var2 ftsh8, suggesting that the protease activity of Type B isomers is completely dispensable, which implies that the chloroplastic FtsH complex has protease sites in excess and that they act redundantly rather than coordinately. However, expression of FtsH2(488) did not fully rescue leaf variegation in var1 var2 because the overall FtsH levels were reduced under this background. Applying an inducible promoter to our complementation analysis revealed that rescue of leaf variegation indeed depends on the overall amount of FtsH. Our results elucidate protein activity and its amount as important factors for the function of FtsH heterocomplexes that are composed of multiple isoforms in the thylakoid membrane.

...THemolysin...




Authors:  

Experiment:X-ray Diffraction With Resolution of 2.00A




     Chains:A

Thermolysin has a molecular weight of 34,600 Da. Its overall structure consists of two roughly spherical domains with a deep cleft running across the middle of the molecule separating the two domains. The secondary structure of each domain is quite different, the N-terminal domain consists of mostly beta pleated sheet, while the C-terminal domain is mostly alpha helical in structure. These two domains are connected by a central alpha helix, spanning amino acids 137-151.[7]
In contrast to many proteins that undergo conformational changes upon heating and denaturation, thermolysin does not undergo any major conformational changes until at least 70 °C.[8] The thermal stability of members of the TLP family is measured in terms of a T50 temperature. At this temperature incubation for 30 minutes reduces the enzymes activity by half. Thermolysin has a T50 value of 86.9 °C, making it the most thermo stable member of the TLP family.[9] Studies on the contribution of calcium to thermolysin stability have shown that upon thermal inactivation a single calcium ion is released from the molecule.[10] Preventing this calcium from originally binding to the molecule by mutation of its binding site, reduced thermolysin stability by 7 °C. However, while calcium binding makes a significant contribution to stabilising thermolysin, more crucial to stability is a small cluster of N-terminal domain amino acids located at the proteins surface.[9] In particular a phenylalanine (F) at amino acid position 63 and a proline (P) at amino acid position 69 contribute significantly to thermolysin stability. Changing these amino acids to threonine (T) and alanine (A) respectively in a less stable thermolysin-like proteinase produced by Bacillus stearothermophillus (TLP-ste), results in individual reductions in stability of 7 °C (F63→T) and 6.3 °C (P69→A) and when combined a reduction in stability of 12.3 °C.[9]



 ...LEuCYL AminOPePtiDase.....


Authors:
Experimet:X-ray Diffraction with Resolution of 2.75A

 Chain:A,B







 The zinc-dependent leucine aminopeptidase from Pseudomonas putida (ppLAP) is an important enzyme for the industrial production of enantiomerically pure amino acids. To provide a better understanding of its structure-function relationships, the enzyme was studied by X-ray crystallography. Crystal structures of native ppLAP at pH 9.5 and pH 5.2, and in complex with the inhibitor bestatin, show that the overall folding and hexameric organization of ppLAP are very similar to those of the closely related di-zinc leucine aminopeptidases (LAPs) from bovine lens and Escherichia coli. At pH 9.5, the active site contains two metal ions, one identified as Mn(2+) or Zn(2+) (site 1), and the other as Zn(2+) (site 2). By using a metal-dependent activity assay it was shown that site 1 in heterologously expressed ppLAP is occupied mainly by Mn(2+). Moreover, it was shown that Mn(2+) has a significant activation effect when bound to site 1 of ppLAP. At pH 5.2, the active site of ppLAP is highly disordered and the two metal ions are absent, most probably due to full protonation of one of the metal-interacting residues, Lys267, explaining why ppLAP is inactive at low pH. A structural comparison of the ppLAP-bestatin complex with inhibitor-bound complexes of bovine lens LAP, along with substrate modelling, gave clear and new insights into its substrate specificity and high level of enantioselectivity.