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The term is defined as having a common evolutionary origin, but it is widely misused to explain the comparison of proteins. A research was done recently [2] to confirm the accuracy of the term usage after the heated argument 20 years ago. Through reviewing hundreds of Pubmed documentations published in , every article with the term homology was read and verified. There is still a misleading idea that homology can be used quantitatively.

Also, interestingly, the error in the terminology was significantly lower in articles with language other than English. Name is derived from parent hydrocarbon by substitution of oic for final e. Phospholipid major class - Constructed of four components, one or more fatty acids, platform to which fatty acids are attached, a phosphate, and alcohol attached to phosphate - Provide hydrophobic barrier, whereas remainder of molecule is hydrophilic which aid to enable interaction with aqueous environment.

Glycolipid, super-containing lipids - Simplest glycolipid is called cerrebroside, which contains single sugar residue glucose or galactose. Membrane formation is a consequence of amphipathic nature of molecules. It helps enable phospholipid to form membrane due to polar head groups favoring contact with water while hydrocarbon tails interact with one another. In a DNA, cytosine will link with tyrosine by triple bonds. Guanine will link with adinine by double bond. Apotosis is a normal process during development and removing cells. These cells can develop to be cancerous cells.

Apoptosis is the programmed death of a cell. It occurs naturally in multicellular organisms and is used to regulate dead cells. Apoptosis occurs daily in human beings destroying naturally anywhere between 20 to 70 billion cells and those cells end up being replaced by newer cells. This orderly pattern of events is called programmed cell death, also known as apoptosis. Apoptosis was discovered by German scientist Carl Vogt who first detailed the events of apoptosis.

This discovery was then later given a more precise definition by Walther Flemming. Since the s apoptosis has started to become more in the mainstream and being investigated more. It truly started in the s when it was seen occurring under the microscope. The picture below is mouse liver cells and the one stained is going through apoptosis. Since the pathway through apoptosis is very long if one biochemical reaction is not carried out it can eventually lead to cells that do not die and go on creating havoc in the organism.

This problem can be linked to the creation of cancer by a malfunctioning cell being able to reproduce and pass on any bad organelles or incorrect DNA sequences. Below is a picture from the Wikimedia Commons briefly showing a depicted drawing of how the apoptosis occurs in the cell:. Apoptosis was studied in roundworms and in the final stages of its cell death, there discovery of the death-inducing protease CED-3 activation became the cause of the apoptosis. In order to regulate these proteases, CSP-3 was discovered to block CED-3 autoactivation and ultimately, to decrease signs of apoptosis during the developmental stages of roundworms.

CSP-3 is a capspase homolog which only works in somatic cells. Therefore, germ cells are not affected by the CSP For example: The withdrawal of growth factors of neurons will cause apoptosis because the growth factors serve as positive signals and are crucial for cell development. Recent researches using mutant mice have helped in understanding of mitochondrial functions of AIF. For example, AIF-deficent mice are used as a model of complex I deficiency which shows a general reprogramming of mitochondrial metabolism. Researches have shown that the uncharacterized splice isoforms of AIF whose tisue and cell type-specific expression pattern can be the cause of some tissue-specific effects in AIF deficiency.

In addition, the failure in detecting AIF mutations might lead to the embryonic lethality of AIF deficiency, which observed in mutant mice. Mutant mice are used in studies of role of AIF in survival, proliferation and metabolism of cells. If level of AIF presence is low, it will not affect the inheritance of Hq mutation and has no major effect in exhibit growth retardation.

An reduction of AIF level over time reduces major effects on the health of aging adult mice. Dorothy Crowfoot Hodgkin is credited with being the founder of protein crystallography. In addition to further developing and refining the technique of X-ray crystallography , she determined the three dimensional structures of pepsin, cholesterol, lactoglobulin, ferritin, tobacco mosaic virus, penicillin, vitamin B, and insulin, among many others.

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She was the first person to discover the shape of a globular protein pepsin , and she won the Nobel Prize in Chemistry for determining the molecular shape of hundreds of molecules. Dorothy Crowfoot graduated from Somerville College of Oxford in with a degree in chemistry. She began her doctoral work at Cambridge in with Dr. Bernal, where she first studied the structural arrangement in atoms of crystals. Further improvements she devised for the technique of X-ray crystallography occurred during her study of cholesterol iodide and over one hundred other steroids. Her accomplishments include the reporting of unit-cell dimensions, recording of reactive indices with respect to their crystallographic axes, which showed the molecules crystal packing, and the elucidation of the hydrogen-bond scheme among atoms.

These techniques were a major breakthrough for legitimizing X-ray crystallography as an accurate analytical technique because her analyses were the first that were based on three dimensional calculations and that established the stereochemistry at each carbon atom. In she returned to Oxford on a research fellowship, where she crystallized and X-ray photographed insulin. To determine its structure, she worked with an isomorphous crystal, a derivative molecule where a single atom is replaced by a heavier one. Thirty four years later, she would finally find success in determining the structure of insulin.

Meanwhile, she received her doctorate from Cambridge University and married Thomas Hodgkin in and began her work on determining the structure of penicillin. She determined that there were three derivatives of benzylpenicillin, sodium, potassium, and rubidium. She used the techniques of isomorphous replacement, optical analogs, and difference maps to elucidate the structure.

Aim & Scope

She also used the first IBM analog computers to do the X-ray calculations, which was the first use of an electronic computer to solve a biochemical problem. Penicillin was instrumental in treating wounded soldiers during World War II, and saved many lives. While completing her penicillin research, Dr. Hodgkin was named a fellow of the Royal Society, Britain's premiere scientific organization, in From to she worked on determining the structure of vitamin B by locating the positions of the heavy atoms, using direct Patterson methods, and then calculating the three-dimensional Fourier series using observed F values and phases based only on the heavy atom's positions.

By pioneering the use of Patterson maps, Dorothy was able to approximate the correct electron density series. In addition to receiving the Royal Medal, she also won a Nobel Prize in Chemistry , making her the third woman to win the Nobel. Albert Claude August 23, - May 22, , who was a Belgium biochemist who specialized in the structure and function of cells was born in Longlier, Belgium and is most well known for winning the Nobel Peace Prize in Physiology and Medicine with Christian de Duve and George Emil Palade "for their discoveries concerning the structural and functional organization of the cell.

Claude was born and buried in Belgium but was also a U.

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He served in World War I with British Intelligence and later received the Inter-Allied Medal for his contributions and was admitted into the University of Liege through a program for war veterans. After receiving his medical degree in , he joined the Rockefeller Institute for Medical Research in New York in and became an American citizen. In Claude discovered the process of cell fractionation. This was groundbreaking at the time because prior to Claude's research, it was thought that the inside of cells were composed of a chaotic mass of substances with no order or particular function.

However, with his discovery, Claude was able to show that cell interiors are in fact very well-organized. To discover cell fractionation, Claude used mechanisms from everyday machinery. He combined the mechanism from meat grinders and a sieve to construct a simple, high-speed centrifuge which led the way for ultracentrifugation, a technique for breaking and spinning infected cells to isolate their agents according to mass. He discovered that particular fractions of the cells correlated to particular cell functions.

Claude discovered the endoplasmic reticulum, which is a membranous network within a cell. The rough endoplasmic reticulum, which has ribosomes attached to the surface, synthesizes proteins. The smooth endoplasmic reticulum synthesizes lipids and steroids, metabolizes carbohydrates and steroids but not lipids , and regulates calcium concentration, drug metabolism, and attachment of receptors on cell membrane proteins. Claude is also coined as one of the first scientists to have used an electronic microscope for his cellular structure studies.

He then went on to retire in De Duve was born on October 2, near London but being of Belgian descent, moved back to Antwerp,Belgium where he was educated by the Jesuits and later went to school at the Catholic University of Leuven. He is most well known for his studies in subcellular biochemistry and cell biology. He was attracted to studying medicine because of the appeal of having an occupation in the field of medicine.

He first started off his career in a laboratory under Professor J. Bouckaert, who greatly influenced his later career. De Duve's work in the laboratory was focused on discovering the effects of insulin upon glucose uptake in the body; therefore, by the time he graduated, de Duve's main primary goal was to elucidate insulin's mechanism of action. From that point on, his career was focused on the biochemical study of insulin. He eventually became a professor in at Louvain, and headed a small research laboratory to answer the broader questions concerning insulin.

In this lab, he accidentally discovered the "latency" of acid phosphatase while investigating carbohydrate metabolism in the liver. He abandoned his insulin focus, and decided to focus on his new discovery instead. Following this new focus in his career, de Duve was coined for discovering lysosomes and peroxisomes, cell organelles where digestive and metabolic processes take place. He found that lysosomes are the cell's digestive system, while peroxisomes are where crucial cell metabolism takes place.

In , de Duve became a professor at Rockefeller University in New York and started another laboratory with the same general research interests as the first laboratory in Belgium. In he was awarded the Nobel Prize with his colleagues Albert Claude and George Palade for describing the structure and function of organelles in cells. In addition to contributing to the discovery of the structures inside cells, he studied the enzyme activity in rat liver cells using a process called rate-zonal centrifugation.

These studies helped pave the way for further discovery into the function of cell structures. Born in Chidambaram in Cuddalore district of Tamil Nadu, India, he spent his life with his highly educated parents. His father headed the biochemistry department at the Maharaj Sayajirao University in Baroda and his mother obtained a Ph. D in psychology. When his mother could not find a position in Baroda's psychology department, she helped his father in his research instead with fellow scientists. They eventually collaborated in their work and greatly influenced Ramakrishnan's scientific interest from a young age.

Through the influence of both his parents, Ramakrishnan became interested in science as a young student, which led him to partake his undergraduate studies in Physics at the same university his parents taught at, Maharaj Sayajirao University in Baroda. He also credits his interest in science being due to a few inspiring teachers and professors from his childhood and his college years.

After completing his graduate studies at Ohio University, he then spend two years studying biology at the University of California, San Diego. While there, Ramakrishnan became interested in ribosomal work while in a lab researching lipid bilayers. He was then offered a postdoctoral position at Don Engelmen and Peter Moore's lab working on a ribosome project involving membrane proteins. His work at Moore's lab taught him the valuable techniques for purifying, reconstituting, and assaying ribosomes, which he would later use to study the structure of the 30S subunit which would win him a Nobel Prize.

It was at this lab that Ramakrishnan first started to map the locations of proteins in the 30S subunit by reconstituting ribosomes where proteins were replaced by deuterated counterparts, as well as learn to map out proteins using neutron scattering experiments at Brookhaven National Laboratory. After an unhappy stay at Oak Ridge's Biology Division, Ramakrishnan found a new position at Brookhaven as a staff scientist where he worked on projects with ribosomes and chromatin. He obtained a tenure to focus on the study of crystallography while on a sabbatical to obtain knowledge to help further his study of ribosomes.

Through some hard work he was able to obtain a position at the Medical Research Council Laboratory of Molecular Biology in Cambridge, England—this laboratory was the birthplace of crystallography. Before leaving to England, Ramakrishnan collected data for ribosomal protein S5 and multiwavelength anamolous diffraction data for crystals of selenomethionyl GH5.

While on his sabbatical in England, he eventually solved the structures of both compounds using the data he brought with him. He eventually decided to move to the LMB to work on his ribosome problem. His focus switched entirely to the 30S subunit structure before this move and the proteins within it were later identified. In , along with Thomas A.

Steitz and Ada E. Yonath, won the Nobel Prize in Chemistry for their studies of the structure and function of the ribosome. Working with crystals and diffraction patterns, Fourier maps were calculated for the structure. The discovery of the 30S subunit structure led to an understanding of how ribosomes can ensure the accuracy of translation when a genetic message is being decoded. His studies have opened new avenues in understanding antibiotic function, along with comprehending the mechanism of tRNA and mRNA recognition and decoding by the ribosome.

Roger David Kornberg was born in April 24th, , and was the Nobel Prize winner of Chemistry in for his research in eukaryotic transcription. Identification of transcription machinery, to Kornberg, was necessary in order to further the study of transcriptional regulation. In addition, yeast was used because it was a unicellular organism that had the same RNA polymerase II system as mammalian systems. Kornberg first accomplished this by creating a technique to form a two-dimensional protein crystal on lipid membranes to produce a low resolution image of the RNA polymerase II.

Later, he was able to use this technique to yield larger crystals that could be used in x-ray crystallography to determine the three-dimensional structure of RNA polymerase II on an atomic level. This technique was then applied to find the other accessory proteins that are associated with RNA polymerase II. He then used this information about the proteins to determine the transcription process of yeast by isolating purified forms of certain proteins in transcription.

She was born in Paris and later moved with her family to New York in She was a research assistant for Elizabeth Russell at Jackson Memorial Laboratory, and shortly attended the University of Rochester for her masters until her father passed a way. After getting married she found a technician position available in the department of biology at Johns Hopkins. As her career developed she eventually studied Hurler's syndrome, an autosomal recessive inherited disease resulting in a multitude of effects including progressive mental retardation and leading to death by about age The biological problem that occurs in those with Hurler's syndrome was known to be associated with the storage and excretion of mucopolysaccharides, though the specifics had yet to be determined.

Patients fibroblasts, synthesizing cells found in connective tissue, showed irregular accumulation of mucopolysaccharides. At first Neufeld thought it to be a problem of overproduction, though her experiments revealed that it was in fact a result of insufficient degradation. After Danes and Bearn published a paper postulating that normal cells assist mutant cells with mucopolysaccharide degradation, Neufeld's partner had a mix up in Hunter's and Hurler's cells in the lab. Keeping this plate with the mixed cells, he and Neufeld discovered that the cells in fact underwent some normalization!

The cells appeared to be secreting 'corrective factors' in mixtures of different genotypes. With these key pieces of knowledge, Neufeld and fellow researches sought therapy for those with Hurler's syndrome. Shull then started a colony of this dog to understand more about this disease, and created an animal model for enzyme replacement therapy.

The Biochemistry of Manganese in Plants | SpringerLink

After short and long term trials with dogs, then 55 human trials, the FDA approved the treatment in for Hurler's syndrome. It was later approved for other mucopolysaccharide storage diseases. Neufeld spent 35 years of her life developing a treatment for the rare lysosomal enzyme disease. Thanks to her, enzyme replacement therapy for alpha-L-Iduronidase deficiency is now an acceptable treatment.

Using the mannose 6-phosphate system, the therapy is now being used to treat Hunter and the Maroteaux-Lamy syndromes. Despite the acceptability of enzyme replacement therapy, there are still many issues. One major issue is that this is a highly expensive treatment, both for administration, and for further research. Another major restriction in this treatment is that not all of the human body is equally receptive to the new enzymes. For example, especially in the central system, intravenously injected enzymes are blocked by the blood-brain barrier.

This is rather unfortunate as many patients with mucopolysaccharide storage diseases have neurologic variations. Though research has been done for alternative administration methods, and other possible pharmaceuticals to correct the enzyme misfolding, as of right now, only the alternative administrations have been brought to clinical trials. Thus it may be many years before the problem is fully solved. Tranplantation of hematopoietic stem cells from bone marrow or cord blood may be another therapy for Hurler syndrome, but it is still a risky procedure. Additionally, it is thought that there might be a "takeover" with the donor's cells gradually replacing the patient's cells.

Since her successful efforts in therapy for Hurler's syndrome, Neufeld has received the Javits Award for her work on Tay-Sachs disease, and is now interested in Sanfiippo Syndrome. Each type of Sanfilippo syndrome has a lysosomal enzyme deficiency, and Neufeld discovered the syndrome to be a tauopathic disease-- a group of neurodegenerative diseases which all lead to dementia. Immunohistochemistry demonstrated that the lysozyme protein was elevated only in the medial entorhinal cortex.

Lysozymes have been studied for a long time, and in fact was one of the first enzymes to be studied, and was discovered to be a product of phagocytes an epithelial cells by Alexander Fleming. However, it had not yet been described in neurons. Neufeld proposed that the elevated levels of the lysozyme in the medial entorhinal cortex could induce hyperphosphorylated tau.

Neufeld hopes that research into Alzheimer's another disease in the tauopathy family will also lead to advancements in understanding and treating Sanfilippo Syndrome. Download from www. For personal use only. Professor Ivan Berke was the founder of the clinic enzymology and medical biochemistry in Serbia and Yugoslavia who played an important role in pharmacy and medicine.

Many students under his tutorship became biochemists who specialized in my different fields. His contribution will help many new generations in the medical field. He was a role model to all of his students in every aspect. Professor Ivan Berke was born on November 13th in Bjelovar. In , he graduated from a Pharmacy Department in Zagreb. In , he graduated from the 7th group of Chemistry In Zagreb. He then served in military for one year. In , he obtained a doctorate in chemistry and was elected to become an assistant at the Chemical Institute of the Faculty of Medicine.

After holding several positions at the Institute of Chemical, he then became director of that Institute. He became a scientific advisor in Budapest and then worked for the Institute of Chemistry in Zagreb until In , he joined the Biochemistry Institute in Belgrade. Later in , he was elected as a Senior Professor of Biochemistry and remained at this position until retirement in His contribution in scientific work was first influenced by Tomislav Pinter, who explained to him about how analytical and physical chemistry worked.

After that, he focused on determining the functional groups of polyterpene acid in a-elemi and b-elemonic acids. This work led to the first papers about the new derivatives of dihydro- and dribromineelemonic acid, and di- and tetrazonide. With the help of Dr Pinter, he focused more about inorganic analytics.

He was the one who created a basis for electrophoresis. This technique became a main focus on clinical biochemistry. Due to financial problems to use the large apparatus in the lab, Dr Berke introduced some methods of solutions for paper electrophoresis. Later then, he was one of the greatest investigators in this field and his works were cited in everything that dealt with this topic. Besides many applications of this electrophoresis, the most interesting study was of nephritic syndrome in children in He spent most of his time doing methodological research in biochemistry and enzymology.

He was a tutor for 18 years during the time he was in Belgrade. More than students under his guidance became biochemists who specialized in my different fields. Throughout his life, he had published many books and articles all over the world. Biochem, J. James C. He is the person who discovered DNA topoisomerase, which was a new enzyme at that time that was able to convert a DNA ring from one form to another. After its discovery, researchers and scientists were able to study how DNA strands and double helixes were passed from one another. Wang was born in the Jiangsu Province of China during a time of war and tension between China and Japan.

Although his time in school was constantly being interrupted, he received a decent education from his mother and through self-learning. Majoring graduating in chemical engineering at the National Taiwan University, he continued to pursue his love for chemistry working as a lecturer after graduation. Back then, scientists answered this questions with two different models - one, because the helical structure of DNA inside and outside a cell were different; or two, because of the unique structure within an intracellular DNA where the two complementary strands were kept apart.

In other words, the first model suggested that an increase in the number of negative supercoils correlated with its size, while the second suggested that the number of negative supercoils would be independent to its size. Wang decided to look into these two models under identical conditions and discovered that a fold range would have a 1.

In an accidental discovery, Wang left centrifuge tubes containing lysate with infected E. From that small incident, Wang later discovered that supercoiled removal activity and DNA ligase did not correlate with each other. Instead, the "w" protein was the one that removed negative supercoils. The s was a time of breakthrough regarding DNA research. James Champoux and Renato Dulbecco discovered an activity in mouse cell that relaxed both negative and positive supercoiled DNA with the presence of Magnesium in , and in , Martin Gellert discovered an E.

In , Wang named these enzymes "topoisomerase" because of their ability to interconvert topological isomers. From there, he was also able to prove that positively supercoiled DNA can be relaxed if a short single-stranded loop is inserted into the DNA. Besides being a successful researcher, Professor Katunuma is also an inspirational colleague and dedicated mentor. His passion for science and intrigued ideas always provoke his coworkers.

Outside his love for structural chemistry, Professor Katunuma is also interested in photography, music and Kendo, or Japanese sword fencing. Professor Nobuhiko Katunuma was born in in Nagasaki, Japan. He graduated from the School of Medicine at Nagoya University in With his widely successful scientific career and dedication to young researchers, Professor Katunuma was promoted to be the Director of the Institute since and also served as Dean of the Medical School at Tokushima University from to Together with his colleague Mitsuko Okada, he discovered mitochondrial glutamicoxalacetic transaminase and the urea cycle glutaminase isoenzymes.

Humus and the chemistry of soil

In , he discovered the acceleration of pyridoxal enzyme turnover in animals with vitamin B6 deficiency and the enzymes participate in proteolysis of the apoproteins. These discoveries suggested that protein degradation can be initiated by the apoprotein formation in proteolysis process. This idea provoke further research into the initiation of various biochemical pathways by limited proteolysis, such as prothrombin activation by mast cell tryptase histamine release by mast cell chymase, and initiation of influenza virus entry by tryptase Clara. In his later years at Tokushima University, he also conducted a research project specialized in the role of lysosomal enzymes and their inhibitors in intracellular proteolysis.

His studies on the 3D structure of protease enzyme cathepsin B in human in collaboration with Robert Huber led to his subsequent studies on chemically designed specific-inhibitors against enzyme cathepsins. With these studies, Professor Katunuma established himself as one of the pioneers in the field of structural based drug synthesis. In his new position as the President of Tokushima Bunri University, Professor Katunuma actively involved in the development of new synthetic cysteine protease inhibitors, the derivatives of E and the CLIK inhibitors, and studied the role of cysteine proteases in bone resorption.

Kido , Hiroshi, and Kazumi Ishidoh. Matthias Hentze is a German scientist born January 25, Had medical training in Germany and the United Kingdom. In , he received his medical degree from the University of Munster in Germany. In the late s did his postdoc at the National Institutes of Health in the United States, where he and his colleagues discovered 'iron-responsive elements'.

Along with his career in science, Hentze is also a marathon runner, and claims that once marathon running became a part of his life, long days no longer wear him down. While doing his postdoct at the National Institutes of Health, Hentze and colleagues discovered 'iron-responsive elements'. This caught his interest in post-transcriptional gene regulation and the diseases of iron metabolism. This interest was the result of a failed postdoctoral project in which Hentze cloned human ferritin genes to try and explain the elusive genetic defect in hereditary hemochromatosis.

This laid the foundation of the first genetic regulatory network that is in cytoplasm. This acts as a bridge between medicine biology and molecular biology. Hentze is a recipient of many national and international research honors such as Germany's highest research award, Gottfried Wilhelm Leibnize Prize.

She is best known for her work with x-ray crystallography and x-ray diffraction images of DNA which eventually led to the discovery of the double helix.

Plant neighbor identity influences plant biochemistry and physiology related to defense

She is most memorable for her contributions to the understanding of DNA. DNA is the foundation of genetics and the better understanding of its structure gives a better understanding of how genetics are endowed from parent to offspring. Although the research and images provided by her proved to be accurate and valuable in discovering the DNA structure, her contributions are often overlooked.

Many of her unpublished drafts show that she located the phosphate groups of DNA. Unfortunately, Watson and Crick only hint at her contribution. In , she died of ovarian cancer while leading research on the polio virus. Franklin was born on July 25, in Notting Hill London into an affluent family. Her father was a merchant banker at the time and her parents had five children, Rosalind being the eldest. According to her mother, Muriel Frances Waley, Rosalind always knew where she was going and at sixteen, she took science for her subject.

At an early age, she demonstrated aptitude for maths and science and foreign languages including French, Italian and German. In , 18 at the time, Rosalind started her college career at University of Cambridge. Three years later, she was awarded a bachelor's degree and received a research fellowship with R.

Norrish at the National Cancer institute. She based her Ph. She worked on DNA fibers and experimental diffraction. Here, she was able to increase her skills with x-ray diffraction.

Journal articles

In Randall's lab, she was partnered with Maurice Wilkins. Although they were both concerned with DNA, they led separate research groups and projects. Although the university was not very welcoming for women, Randall persisted on the DNA project and utilized her knowledge in x-ray crystallography to see different images of the DNA. Franklin was an X-ray crystallographer. Her work had confirmed that the DNA is of a helical structure. Furthermore, she determined the location of the phosphate groups and insisted that the backbones were on the outside of the structure.

Although she was very close to solving the complete structure of DNA, Watson and Crick beat her to the finish due to many bickers with Wilkins and herself. It is known that at one point, Wilkins showed Watson one of Franklin's x-ray portraits of the DNA and this served as the last missing puzzle piece for Watson and Crick. Although Franklin's work was mentioned in the published journal written by Watson and Crick, the amount of credit she deserves still remains questionable. Although she did have a meaningful role in proposing the structure of the DNA, many people argue that Watson and Crick already figured out the model on their own and that her portrait just 'confirmed' what they already knew.

Instead of inviting Franklin to co-author their paper describing the structure, Watson and Crick invited Wilkins, who leaked Franklin's portrait to Watson, to co-author. Although Wilkins declined this offer, he later expressed his regret of denying this offer. She was never nominated for a Nobel Prize because she died of cancer in Instead, the prize subsequently went to Watson, Crick, and Wilkins.

It was extraordinary that her data was shown without her knowledge to researchers at another institute and Watson and Crick later admitted that without that data they could not have completed the proof of their model. Shigeru Tsuiki was one of the pioneers in the research fields of complex carbohydrates and protein phosphatases. In , after graduated from the Tohoku University Medical School of Japan, he began his career as a biochemist by working in the laboratory. Five years later, he had a chance to visit Dr Ward Pigman- a professor at the University of Alabama Birmingham Medical School after getting his PhD degree, and his contribution began from here.

During his prominent career, he accomplished three different outstanding contributions to the biochemistry research field: with the method of purifying mucin from bovine submaxillary glands, identification of four different molecular species of mammalian sialidase, and an establishment of molecular basis for mammalian protein phosphatases. Science New York, N. A journal article with 2 authors. Strausberg, R. From knowing to controlling: a path from genomics to drugs using small molecule probes.

A journal article with 3 authors. Karan, S. Sub nm polyamide nanofilms with ultrafast solvent transport for molecular separation. A journal article with 4 or more authors. Cohen, G. Reducing the racial achievement gap: a social-psychological intervention. Martinelli, R. Program Management for Improved Business Results. Springer International Publishing, Cham. Michels, J.

Springer International Publishing, Cham, pp. Andrew, E.