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DNA Techology

Saturday, May 29, 2010 11:21 PM By surendra , In


DNA technology has revolutionized modern science. Deoxyribonucleic acid (DNA), or an organism's genetic material—inherited from one generation to the next—holds many clues that have unlocked some of the mysteries behind human behavior, disease, evolution, and aging. As technological advances lead to a better understanding of DNA, new DNA-based technologies will emerge. Recent advances in DNA technology including cloning, PCR, recombinant DNA technology, DNA fingerprinting, gene therapy, DNA microarray technology, and DNA profiling have already begun to shape medicine, forensic sciences, environmental sciences, and national security.

In 1956, the structure and composition of DNA was elucidated and confirmed previous studies more than a decade earlier demonstrating DNA is the genetic material that is passed down from one generation to the next. A novel tool called PCR (polymerase chain reaction) was developed not long after DNA was descovered. PCR represents one of the most significant discoveries or inventions in DNA technology and it lead to a 1993 Nobel Prize award for American born Kary Mullis (1949–).
PCR is the amplification of a specific sequence of DNA so that it can be analyzed by scientists. Amplification is important, particularly when it is necessary to analyze a small sequence of DNA in quantities that are large enough to perform other molecular analyses such as DNA sequencing. Not long after PCR technology was developed, genetic engineering of DNA through recombinant DNA technology quickly became possible. Recombinant DNA is DNA that has been altered using bacterial derived enzymes called restriction endonucleases that act like scissors to cut DNA. The pattern that is cut can be matched to a pattern cut by the same enzymes from a different DNA sequence. The sticky ends that are created bind to each other and a DNA sequence can therefore be inserted into another DNA sequence.

Restriction endonucleases are also important in genetic fingerprinting. In this case, enzymes that recognize specific DNA sequences can produce fragments of DNA by cutting different parts of a long strand of DNA. If there are differences in the sequence due to inherited variation—meaning that there are extra DNA or specific sequences altered such that the restriction enzymes no longer recognize the site, variable patterns can be produced. If these patterns are used to compare two different people, they will have a different fragment pattern or fingerprint. Genetic fingerprinting can be used to test for paternity. In forensics, genetic fingerprinting can be used to identify a criminal based on whether their unique DNA sequence matches to DNA extracted from a crime scene. This technology can also allow researchers to produce genetic maps of chromosomes based on these restriction enzyme fingerprints. Becasue there are many different enzymes, many different fingerprints can be ascertained

Recombinant DNA technology can also be applied to splicing genes into molecular devices that can transport these genes to various cellular destinations. This technique, also called gene therapy, has been used to deliver corrected genes into individuals that have defective genes that cause disease. Gene splicing has also been applied to the environment as well. Various bacteria have been genetically modified to produce proteins that break down harmful chemical contaminants such as DDT. Currently, scientists are investigating the application of this technology to produce genetically engineered plants and crops that can produce substances that kill insects. Similarly, fruits can be engineered to have genes that produce proteins that slow the ripening process in an effort to extend their shelf life.

DNA microarray technology, also known as the DNA chip, is the latest in nanotechnology that allows researchers the have ability to study the genome in a high throughput manner. It can be used for gene expression profiling which gives scientists insights into what genes are being up or down-regulated. Various genetic profiles can be determined in order to estimate cancer risk or to identify markers that may be associated with disease. It has the ability only to detect changes in gene expression that are large enough to be detected above a baseline level. Therefore, it does not detect subtle changes in gene expression that might cause disease or play a role in the development of disease. It can also be used for genotyping, although clinical diagnostic genotyping using microarray technology is still being investigated.

Genes from other species can also be used to add new traits to a particular organism. For example, bacteria, mice, and plants have all had luminescent (light glowing) genes from jelly fish added to their genomes. Another reason for adding genes to a foreign organism is to manufacture various nutritional or pharmaceutical products. Some cows have been modified so that they can produce human insulin or vitamins in their milk in bulk. Pigs have been modified to overcome a number of transplantation problems so that some limited transplantation of organs can be carried out from pigs to humans, also called xenotransplation.

DNA technology is a relatively new area of research with enormous controversy. It will likely continue to be a large part of public debate and have an impact on every aspect of medical diagnostics, therapeutics, forensics, and genetic profiling.
READ MORE ABOUT PROTEOMIC

PROTEOMICS

Wednesday, May 26, 2010 8:41 AM By surendra , In


1. INTRODUCTION TO PROTEOMICS

Proteomics is the large-scale study of proteins, particularly their structures and functions. Proteins are vital parts of living organisms, as they are the main components of the physiological metabolic pathways of cells. The term "proteomics" was first coined in 1997 to make an analogy with genomics, the study of the genes. The word "proteome" is a blend of "protein" and "genome", and was coined by Prof Marc Wilkins in 1994 while working on the concept as a PhD student.
Proteome: All the proteins that can be synthesized by the cell.
The proteome is the entire complement of proteins, including the modifications made to a particular set of proteins, produced by an organism or system. This will vary with time and distinct requirements, or stresses, that a cell or organism undergoes.
A proteome is quite a bit more complicated than the genome because a single gene can give rise to a number of different proteins through
alternative splicing of the pre-messenger RNAs;
RNA editing of the pre-messenger RNAs;
attachment of carbohydrate residues to form glycoprotein;
addition of phosphate groups to some of the amino acids in the protein
While we humans may turn out to have only 25 to 30 thousand genes, we probably make at least 10 times that number of different proteins. More than 50% of our genes produce pre-mRNAs that are alternatively-spliced.



2. INTRODUCTION TO GENOMICS

Genomics is the study of the genomes of organisms. The field includes intensive efforts to determine the entire DNA sequence of organisms and fine-scale genetic mapping efforts. The field also includes studies of intragenomic phenomena such as heterosis, epistasis, pleiotropy and other interactions between loci and alleles within the genome. In contrast, the investigation of the roles and functions of single genes is a primary focus of molecular biology and is a common topic of modern medical and biological research. Research of single genes does not fall into the definition of genomics unless the aim of this genetic, pathway, and functional information analysis is to elucidate its effect on, place in, and response to the entire genome's networks.
For the United States Environmental Protection Agency, "the term "genomics" encompasses a broader scope of scientific inquiry associated technologies than when genomics was initially considered. A genome is the sum total of all an individual organism's genes. Thus, genomics is the study of all the genes of a cell, or tissue, at the DNA (genotype), mRNA (transcriptome), or protein (proteome) levels.


3. Why study Proteomics?
The study of proteomics is important because proteins are responsible for both the structure and the functions of all living things. Genes are simply the instructions for making proteins. It is proteins that make life.
The key requirement in understanding protein function is to learn to correlate the vast array of potential protein modifications to particular phenotypic settings, and then determine if a particular post-translational modification is required for a function to occur.
Even if one is studying a particular cell type, that cell may make different sets of proteins at different times, or under different conditions. Furthermore, as mentioned, any one protein can undergo a wide range of post-translational modifications.
Therefore a "proteomics" study can become quite complex very quickly, even if the object of the study is very restricted. In more ambitious settings, such as when a biomarker for a tumor is sought - when the proteomics scientist is obliged to study sera samples from multiple cancer patients - the amount of complexity that must be dealt with is as great as in any modern biological project.
3.1 Limitations to genomic study
Scientists are very interested in proteomics because it gives a much better understanding of an organism than genomics. First, the level of transcription of a gene gives only a rough estimate of its level of expression into a protein. An mRNA produced in abundance may be degraded rapidly or translated inefficiently, resulting in a small amount of protein. Second, as mentioned above many proteins experience post-translational modifications that profoundly affect their activities; for example some proteins are not active until they become phosphorylated. Methods such as phosphoproteomics and glycoproteomics are used to study post-translational modifications. Third, many transcripts give rise to more than one protein, through alternative splicing or alternative post-translational modifications. Fourth, many proteins form complexes with other proteins or RNA molecules, and only function in the presence of these other molecules. Finally, protein degradation rate plays an important role in protein content.

4. Methods of studying proteins
4.1 Determining proteins which are post-translationally modified
One way in which a particular protein can be studied is to develop an antibody which is specific to that modification. For example, there are antibodies which only recognize certain proteins when they are tyrosine-phosphorylated; also, there are antibodies specific to other modifications. These can be used to determine the set of proteins that have undergone the modification of interest.
For sugar modifications, such as glycosylation of proteins, certain lectins have been discovered which bind sugars. These too can be used.
A more common way to determine post-translational modification of interest is to subject a complex mixture of proteins to electrophoresis in "two-dimensions", which simply means that the proteins are electrophoresed first in one direction, and then in another... this allows small differences in a protein to be visualized by separating a modified protein from its unmodified form. This methodology is known as "two-dimensional gel electrophoresis".
Recently, another approach has been developed called PROTOMAP which combines SDS-PAGE with shotgun proteomics to enable detection of changes in gel-migration such as those caused by proteolysis or post translational modification.

4.2 Determining the existence of proteins in complex mixtures
Classically, antibodies to particular proteins or to their modified forms have been used in biochemistry and cell biology studies. These are among the most common tools used by practicing biologists today.
For more quantitative determinations of protein amounts, techniques such as ELISAs can be used.
For proteomic study, more recent techniques such as Matrix-assisted laser desorption/ionization have been employed for rapid determination of proteins in particular mixtures.
4.3 How To Study?(A Procedure)
1. Isolate a homogeneous population of cells (e.g., yeast cells that have just been switched from glucose to galactose as their energy source).
2. Extract the contents of the cells and separate the mix of proteins from other components.
3. Separate the proteins in the mix by two-dimensional (2D) gel electrophoresis. This separates the proteins
o in one dimension by their electrical charge;
o in the second dimension by their size.
(The procedure is analogous to that used in paper chromatography.
4. Stain the gel to visualize the various spots of protein.
5. Punch out a spot.
6. Add a protease (e.g., trypsin) to digest the protein in that spot into a mix of peptides.
7. Run the mix through a mass spectrometer, which will separate the peptides into sharply-defined peaks.
8. Run the resulting data through a database of all known proteins (that have been digested with the same enzyme) to see if you can find a match.

What if there is no match; that is, you have stumbled on an unknown protein?
1. Isolate individual peptides from your mix and run one through a mass spectrometer that has been modified to
o first randomly break the peptide into a mix of fragments containing one, two, etc. amino acids
o then measure the mass of each fragment.
2. Enter the resulting data into a database that matches the mass data with known pairs, triplets, etc. of amino acids.
3. With the aid of overlaps, assemble the fragments to reveal the entire sequence of the peptide.
4. "Back-translate" the amino acid sequence to determine what sequence of nucleotides in DNA could encode that peptide.
5. Search the genome database for an open reading frame (ORF) that contains that sequence.
6. Translate that ORF to get the entire amino acid sequence of your protein.
4.4 Study of Three-Dimensional (3D) Structure of a Protein
The clearest picture of how different proteins interact with one another to form functional complexes will come from determining the 3D structure of the complex. There are two methods:
X-ray crystallography;
nuclear magnetic resonance (NMR) spectroscopy.
X-ray crystallography requires that you be able to crystallize the protein. This is often a difficult task and especially difficult for complexes of two or more proteins.
Although in both cases the proteins are binding to DNA, they are also binding to each other (as homodimers).
NMR spectroscopy has been especially useful in producing 3D images of proteins that cannot be crystallized.
5. Practical applications of proteomics
One of the most promising developments to come from the study of human genes and proteins has been the identification of potential new drugs for the treatment of disease. This relies on genome and proteome information to identify proteins associated with a disease, which computer software can then use as targets for new drugs. For example, if a certain protein is implicated in a disease, its 3D structure provides the information to design drugs to interfere with the action of the protein. A molecule that fits the active site of an enzyme, but cannot be released by the enzyme, will inactivate the enzyme. This is the basis of new drug-discovery tools, which aim to find new drugs to inactivate proteins involved in disease. As genetic differences among individuals are found, researchers expect to use these techniques to develop personalized drugs that are more effective for the individual.
A computer technique which attempts to fit millions of small molecules to the three-dimensional structure of a protein is called "virtual ligand screening". The computer rates the quality of the fit to various sites in the protein, with the goal of either enhancing or disabling the function of the protein, depending on its function in the cell. A good example of this is the identification of new drugs to target and inactivate the HIV-1 protease. The HIV-1 protease is an enzyme that cleaves a very large HIV protein into smaller, functional proteins. The virus cannot survive without this enzyme; therefore, it is one of the most effective protein targets for killing HIV.
5.1 Biomarkers
Understanding the proteome, the structure and function of each protein and the complexities of protein-protein interactions will be critical for developing the most effective diagnostic techniques and disease treatments in the future.
An interesting use of proteomics is using specific protein biomarkers to diagnose disease. A number of techniques allow to test for proteins produced during a particular disease, which helps to diagnose the disease quickly. Techniques include western blot, immunohistochemical staining, enzyme linked immunosorbent assay (ELISA) or mass spectrometry.

medical college in eastern nepal

12:11 AM By surendra , In


Nobel Medical College Teaching Hospital and Research Centre School is a non governmental medical college which was established in 2005 in joint collaboration and affiliation from Kathmandu University and the Medical Degree is recognized by the Nepal Medical Council.
Educational strategy is based on Problem-Based Learning (PBL) and community-Based Learning (CBL). as an integrated part of the curriculum. PBL comprises small group tutorial sessions under the guidance of faculty tutor. Following this, self directed, independent learning takes place. This is supplemented by laboratory experiments and lectures on selected key topics. CBL comprises of teaching/Learning in community with regular residential posting as well as the usual classroom learning.
NMCTHRC has been recognized by the Nepal Medical Council


Medical College
The Basic Science Campus
The Basic Science Campus in the premises of Nobel Hospital & Research Center P. Ltd. Kanchanbari, Biratnagar, has been approaching completion in construction for Basic Science Disciplines like Anatomy, Physiology, Pharmacology and Community Medicine. The teaching learning facilities for disciplines like Biochemistry, Pathology and Microbiology now running in the Basic Science Campus in Kanchanbari, Biratnagar.

ADMISSION AT NOBEL MEDICAL COLLEGE:
Nepali students have to qualify for KUMET
(Entrance Test conducted by Kathmandu University) for admission.
Expatriate students and students from SAARC nations shall appear for the admission test at the College itself.
The candidates can obtain the Prospectus with Application Form at The Nobel Medical College Teaching Hospital, Kanchanbari, biratnagar-5,Nepal by paying NRs 1000.00 for Nepalese students or IRS 1000.00.for Indian students or students from SAARC nations in cash at Medical College counter or A/C draft payable at Bank Of Kathmandu / Nabil Bank Limited on behalf of The Nobel Medical College Teaching Hospital P. Ltd.

Duly filled in applications along with attested photocopies of School Leaving Certificate, ISc/CBSC Certificate or 10+2 Certificate, Character Certificate from the Chief of the Institution last attended, Nationality/Citizenship Certificate, Identification Certificate, Valid Passport ( In case of students from SAARC countries) have to be submitted. The Migration Certificate have to be submitted at the time of admission if the student has passed the Class XII Examination from university other than the Kathmandu University.

Manipal College of Medical Sciences

Monday, May 24, 2010 12:11 AM By surendra

Manipal College of Medical Sciences is the first private medical school in Nepal. Established in 1994 and located in Pokhara, the school is affiliated with Kathmandu University. The school is the result of a collaboration between the Manipal Education and Medical Group (MEMG) and the Government of Nepal.
MCOMS has two locations in one of the most beautiful cities in Nepal, Pokhara. The basic sciences campus is located at Deep Heights, and 1st and 2nd year courses are taught there. The clinical campus with the teaching hospital is located in Fulbari, Pokhara, over looking the Annapurna mountain range.
Courses
• MBBS
• PCL Nursing B.SC. Nursing (Since 2009)
MBBS
It is considered as the best private medical college in Nepal. 75 students are enrolled biannually. The majority of the students are of Indian and Nepalese origin. Students from other nations such as: Sri Lanka, United States of America, Canada, New Zealand, Kenya, etc are also enrolled. Many elective students visit from American and European Universities and have the opportunity for hands on training as well as indulging in the beauty and serenity of Nepal. It is one of the best choices amongst medical colleges in Nepal.
The course is divided into 9 semesters, each of 6 months duration (4.5 years). The first four semesters are devoted to the basic sciences.
The basic science training takes place at Deep Campus. Only after passing all the subjects of basic sciences, a student is promoted to the clinical aspect of the course.
The next five semesters are devoted to the study of clinical sciences, and are held at Manipal Teaching Hospital, Pokhara.
It is recognized by the Medical Council of Nepal, SriLanka, and other countries. It is also listed in WHO List and also recognized under FAIMER.
Hospital
Manipal Teaching Hospital (MTH) is a 700-bed hospital, located at Phulbari; Pokhara.It is a 5-storey building. With housing facilities available on campus

Best doctors producer in Nepal

Sunday, May 23, 2010 11:56 PM By surendra , In

Best doctors producer in Nepal

Maharajgunj campus

Maharajgunj Campus (MC) at Maharajgunj, Kathmandu is one of the nine campuses of the Institute of Medicine (IoM). Since its upgradation to the status of a campus of IoM from the Auxiliary Health Worker's School in 1972, MC has, during the span of just over two decades, played a significant role in conducting academic programmes for the development of different categories of Human Resources for Health (HRH) in Nepal. Of the twenty-nine academic programmes that the IoM runs to date, twenty-five consisting of eighteen postgraduate, four undergraduate and three certificate programmes (about ninty percent of the educational activities of the IoM) are being conducted at MC. In its endeavour to create competent and diverse Human Resources for Health. HRH, ranging from a Primary health Care worker to a Medical Specialist for rendering primary to tertiary health care in the country. MC has indeed taken a long stride in the field of medical education in Nepal.

The establishment of Tribhuvan University Teaching Hospital (TUTH) in 1983 near to MC premise, made the fact very clear imparting medical education does require a teaching hosital for facilitating teaching-learning activities effectively. With the establishment of TUTH, MC acquired the full status of the First Medical School in Nepal. Since then, MC not only became responsible for imparting medical education but also started to provide tertiary health care to all those coming to THTH. The faculty of medicine here played a dual role- that of a medical teacher and a medical specialist.

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