www.knowyourmedicine.gov.my

REVIEW

Medicines are chemical substances that are used for treatment, prevention and diagnosing diseases. It 

is important to know what is your medicine is called and what it looks like.  Some medicine may look similar although they have different names and uses. Medicine can be prescribed by its brand name or chemical name. 

For futher explaination you can browse to this website www.knowyourmedicine.gov.my

 

This website will assist us to know more about our medicine. For example we can search the name of our medicine, the medicine is for what diseases, we can also make a search about common diseases like high blood pressure, diarrhea, constipation and etc.

"KNOW YOUR MEDICINE" is a campaign that have been organized by the Ministry Of Health (MOH) and the Consumer Association of Malaysia (Fomca). It was initiated in view of irrational use of medicines which is not only danger to public health but also has adverse impact on the economy. 

Moreover, we also can take a look for National Medicines Policy and the Liaison Officers all around the Malaysia. As a pharmacist student, this website is very useful for us because it help us to know more about medicine and medical field. 

As for the consumer, it is really helping because it help them to know more about their medicine. There is an animation on how to consume medicine correctly and the quality use of medicine. It also provide us the information on how to detect a genuine Meditag Hologram. There is also related search for products registered by Drug Control Authority (DCA) so consumer can check the healthy product that have been marketed is already registered or not. Consumers also can check their BMI using the "BMI Calculator" that have been provided in the website. There is lot of information in this website that can is really useful for consumer.

Review NPCB

Biro Pengawalaan Farmaseutikal Kebangsaan (BPFK) or also known as National Pharmaceutical Control Bureau (NPCB), was set up in October 1978 under the quality control activity of Pharmacy and Supply Programme. This institution was established to implement quality control on pharmaceutical products. The infrastructure and facilities were designed to meet the requirements for testing and quality control activities.

It is a system to monitor products in the market was set-up. Information on drugs to medical profession and consumer was made available through a drug information service. The NPCB also handles courses and provides training to personnel from the ASEAN countries, for example from Sri Lanka, Bangladesh, Myanmar and Vietnam. NPCB also was given an international recognition by the World Health Organisation(WHO).

Official portal website: https://www.bpfk.gov.my/‎

Human Genome Project

The Human Genome Project (HGP) was one of the great feats of exploration in history an inward voyage of discovery rather than an outward exploration of the planet or the cosmos; an international research effort to sequence and map all of the genes together known as the genome of members of our species, Homo sapiens.
The HGP was the international, collaborative research program whose goal was the complete mapping and understanding of all the genes of human beings. All our genes together are known as our genome.
The HGP was the natural culmination of the history of genetics research. The hereditary material of all multi-cellular organisms is the famous double helix of deoxyribonucleic acid (DNA), which contains all our genes. DNA, in turn, is made up of four chemical bases, pairs of which form the "rungs" of the twisted, ladder-shaped DNA molecules. All genes are made up of stretches of these four bases, arranged in different ways and lengths. HGP researchers have deciphered the human genome in three major ways: determining the order, or sequence of all the bases in our genome's DNA; making maps that show the locations of genes for major sections of all our chromosomes; and producing what are called linkage maps, complex versions of the type originated in early Drosophila research, though which inherited traits such as those for genetic disorder can be tracked over generations.
The HGP has revealed that there are probably about 20,500 human genes. The completed human sequence can now identify their locations. The ultimate product of the HGP has given the world a resource detailed information about the structure, organization and function of the complete set of human genes. The tools created through the HGP also continue to inform efforts to characterize the entire genomes of several other organisms used extensively in biological research, such as mice, fruit flies and flatworms.
These ambitious goals required and will continue to demand a variety of new technologies that have made it possible to relatively rapidly construct a first draft of the human genome and to continue to refine the draft. These techniques include DNA sequencing, Yeast Artificial Chromosomes (YAC), Bacterial Artificial Chromosomes (BAC), the polymerase chain reaction (PCR) and electrophoresis.

 

 

PROTEIN STRUCTURE MOVIE

ABOUT US

Hi there, I am Sathi Periakaruppan. Together with me here, my friends Dheviya Rajendran and Nurul Shahira. We are doing our Bachelor in Pharmacy at Management & Science University (MSU). 

Basically, we love dealing with drugs and chemicals. That's the reason we chose pharmacy as our future career. We spend our time mostly in the library to gain knowledge and stay updated. 

Most importantly, we love books. We even go to the National Library to refer to pharmacy related books to gain more information which can be helpful in the class. We find it fun and interesting to study about drugs and chemicals.

Myself Sathi, I'm from Shah Alam whereas Dheviya from Banting and Shahira from Kajang. We feel blessed and lucky to be in MSU, where the lecturers are very friendly and helpful. They help us with our studies at any time. We are very delighted to join here and further our studies. We found studying bioinformatics in pharmacy very interesting and our lecturer Mr. Ibrahim is a very down to earth and warmhearted person. 

PROTEIN STRUCTURE

Protein Structure

There are four distinct levels of protein structure.Each α-amino acid consists of a backbone part that is present in all the amino acid types, and a side chain that is unique to each type of residue. An exception from this rule is proline. Because the carbon atom is bound to four different groups it is chiral, however only one of the isomers occur in biological proteins. Glycine however, is not chiral since its side chain is a hydrogen atom. A simple mnemonic for correct L-form is "CORN": when the C_α atom is viewed with the H in front, the residues read "CO-R-N" in a clockwise direction.

THE PRIMARY STRUCTURE

The primary structure refers to amino acid linear sequence of the polypeptide chain. The primary structure is held together by covalent bonds such as peptide bonds, which are made during the process of protein biosynthesis or translation. The two ends of the polypeptide chain are referred to as the carboxyl terminus (C-terminus) and the amino terminus (N-terminus) based on the nature of the free group on each extremity. Counting of residues always starts at the N-terminal end (NH₂-group), which is the end where the amino group is not involved in a peptide bond. The primary structure of a protein is determined by the gene corresponding to the protein. A specific sequence of nucleotides in DNA is transcribed into mRNA, which is read by the ribosome in a process called translation. The sequence of amino acids was discovered by F. Sanger. The sequence of a protein is unique to that protein, and defines the structure and function of the protein. The sequence of a protein can be determined by methods such as Edman degradation or tandem mass spectrometry. Often however, it is read directly from the sequence of the gene using the genetic code. We know that there are over 10,000 proteins in our body which are composed of different arrangements of 20 types of amino acid residues (it is strictly recommended to use the word "amino acid residues" as when peptide bond is formed a water molecule is lost so, protein is made up of amino acid residues). Post-translational modifications such as disulfide formation, phosphorylations and glycosylations are usually also considered a part of the primary structure, and cannot be read from the gene. Example: Insulin is composed of 51 amino acids in 2 chains. One chain has 31 amino acids and the other has 20 amino acids.

THE SECONDARY STRUCTURE

Secondary structure refers to highly regular local sub-structures. Two main types of secondary structure, the alpha helix and the beta strand or beta sheets, were suggested in 1951 by Linus Pauling and coworkers. These secondary structures are defined by patterns of hydrogen bonds between the main-chain peptide groups. They have a regular geometry, being constrained to specific values of the dihedral angles ψ and φ on the Ramachandran plot. Both the alpha helix and the beta-sheet represent a way of saturating all the hydrogen bond donors and acceptors in the peptide backbone. Some parts of the protein are ordered but do not form any regular structures. They should not be confused with random coil, an unfolded polypeptide chain lacking any fixed three-dimensional structure. Several sequential secondary structures may form a "supersecondary unit".

THE TERTIARY STRUCTURE

Tertiary structure refers to three-dimensional structure of a single,double,or triple bonded protein molecule. The alpha-helixes and beta pleated-sheets are folded into a compact globular structure. The folding is driven by the non-specific hydrophobic interactions (the burial of hydrophobic residues from water), but the structure is stable only when the parts of a protein domain are locked into place by specific tertiary interactions, such as salt bridges, hydrogen bonds, and the tight packing of side chains and disulfide bonds. The disulfide bonds are extremely rare in cytosolic proteins, since the cytosol is generally a reducing environment.

THE QUATERNARY STRUCTURE

Quaternary structure is the three-dimensional structure of a multi-subunit protein and how the subunits fit together. In this context, the quaternary structure is stabilized by the same non-covalent interactions and disulfide bonds as the tertiary structure. Complexes of two or more polypeptides (i.e. multiple subunits) are called multimers. Specifically it would be called a dimer if it contains two subunits, a trimer if it contains three subunits, and a tetramer if it contains four subunits. The subunits are frequently related to one another by symmetry operations, such as a 2-fold axis in a dimer. Multimers made up of identical subunits are referred to with a prefix of "homo-" (e.g. a homotetramer) and those made up of different subunits are referred to with a prefix of "hetero-" (e.g. a heterotetramer, such as the two alpha and two beta chains of hemoglobin).