Supramolecular chemistry actually represents a fairly simple concept.“In contrast to molecular chemistry, which is predominantly based on the covalent bonding of the atoms, supramolecular chemistry is based up on intermolecular interactions, i.e on the association of two or more building blocks, which are held together by intermolecular forces”. When molecules get larger, they have the ability to stick together and that allows the formation of larger assemblies of molecules that are not bonded to one another but stick together and organize themselves, just like the pieces of the puzzle. Supramolecular chemistry is the domain of chemistry that deals with the forces that will allow them to stick together, which may include hydrogen bonding, metal coordination, hydrophobic forces, van der Waals forces pi-pi interactions and electrostatic effects. Important concepts that make this domain of chemistry very special include molecular self-assembly, folding, molecular recognition, host-guest chemistry, mechanically-interlocked molecular architectures, and dynamic covalent chemistry.
1.1.1 Supramolecular self-assembly:
Supramolecular self-assembly has wider applications in sciences (like Genetic engineering, Pharmaceutical research and Bio-Nanotechnology) that deal with living systems. Living systems stand out as a typical example for supramolecular assemblies.
Individual cells spontaneously self assemble in to functional entities when they divide, and learning the rules of self assembly, that gives rise to functionality will help the scientific community to find a variety of applications.
Most of the infectious diseases are dependent on the ability to assemble in to functional entities. Functional viruses are a self-assembly process...
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....U398p_ldU0cThe design porphyrin based receptors for the recognition of anions is a difficult area in Supramolecular chemistry.Recently a lot of research have been started and the results obtained so far are very promising. www.princeton.edu/chemistry/macmillan/group-meetings/HK_anionic%20binding.pdf: Design of Porphyrin Anion Receptors:
Considering a design is of utmost important before an anion receptor can be synthesized.The receptors must be preorganised for substrate binding. The amide and urea groups should be organized in such a position allowing them to converge the anion.Improved binding results by providing a maximum number of hydrogen bonding contacts for the anionic guests.The design should be in such a way that it makes the compound synthetically accessible in large yields so that various studies can be carried out.
In 1989, Fogleman et al. analyzed the uncoating and penetration of Simian virus (SV 40). It uses the ganglioside...
Bloodborne pathogens are viruses that deteriorate cells within the body. A virus is a submicroscopic parasitic organism that feeds on cells. Viruses are dependent on cells for their nutrients so the virus survive and reproduce. Every virus consists of either deoxyribonucleic acid (DNA) or ribonucleic acid (RNA). A virus can contain a strand of one or the other, but not both. This RNA or DNA is contained within a protein shell for protection. A virus is a parasite that is dependent upon cells for metabolic and reproductive requirements. By using the cell the virus makes the host very ill by redirecting cellular activity to make more viruses.
Viruses are the simplest and tiniest of microbes, and are made up of proteins, nucleic acid, and lipids. The nucleic acids contain the genetic code that helps them grow and reproduce, but only once they find their way into a living organism. Viruses themselves are not considered living organisms because they don’t have cells, they don’t metabolize nutrients, produce and excrete wastes, and they can’t move around on their own. The remains of the nucleic acid then forms a covering, called the capsid. Once the capsid gets removed, viruses use the building materials of th...
One thing that must be noted is that contrary to popular belief, infectious agents such as viruses, bacteria, parasites, etc. are not desig...
The virus is primarily spherical shaped and roughly 200nm in size, surrounded by a host-cell derived membrane. Its genome is minus-sense single-stranded RNA 16-18 kb in length. It contains matrix protein inside the envelope, hemagglutinin and neuraminidase, fusion protein, nucleocapsid protein, and L and P proteins to form the RNA polymerase. The host-cell receptors on the outside are hemagglutinin and neuraminidase. The virus is allowed to enter the cell when the hemagglutinin/ neuraminidase glycoproteins fuse with the sialic acid on the surface of the host cell, and the capsid enters the cytoplasm. The infected cells express the fusion protein from the virus, and this links the host cells together to create syncitia.
Thus, it contains two active sites and has metal ions that play a key role in regulating catalytic activities and stabilizing enzyme-substrate complex. The active sites are 30Å apart from each other (7). As proposed by Gettins and Coleman using NMR studies (6), each active site of AP comprises of three metal binding sites, which acknowledged as M1, M2, and M3. Two zinc ions bind to M1 and M2 sites while a magnesium ion occupies M3. In each active site, two zinc ions are 4Å apart while magnesium ion is 5Å and 7Å away from two zinc ions (7). The structures of AP are shown in Figure 1, which specifically indicating metal binding sites and interaction with essential amino acids in active
...ving things carry viruses in their cells. Even fungi and bacteria and inhabited by viruses and are occasionally destroyed by them. A virus makes copies of itself in a cell until eventually the cell gets pigged with virus and pops and the viruses spill out of the broken cell. If enough cells are destroyed, such as they do in the case of Ebola, the host dies. A virus does not "want" to kill its host. That is not in the best interest of the virus, because then the virus may also die, unless it can jump fast enough out of the dying host into a new host.
This is made possible by the use of enzymes. Enzymes essentially work within the cells and their ability determined as a result of their specificity brought about by the shapes from the amino acid sequences (Daniel and Danson 2740).
...Coauthor, ChemBioChem 2006, 7, 1-10; b) A. Author, B. Coauthor, Angew. Chem. 2006, 118, 1-5; Angew. Chem. Int. Ed. 2006, 45, 1-5.))
The Ebola virus is also a part of the Filoviridae family, along with Marburg, and contains a lipid envelope and has a single RNA strand. Ebolavirons are approximately 80 nanometers in width and vary in length. They also contain seven structural proteins that are surrounded by the lipid envelope that has an attached glycoprotein. During replication, it goes through translation but during transcription it stops after one or two genes so that on the 3 prime end it is completely transcribed but the 5 prime end is not transcribed and does not possess a 5-cap.
Figure 3 shows the structure of the prepared protein along with the ligand depicted in green colour.
The term macromolecules is sometimes used to refer to aggregates of two or more macromolecules held together by intermolecular forces rather then by chemical bonds. Another common macromolecule property that does not characterize smaller molecules is the need for assistance in dissolving into solution. Many require salts or particular ions to dissolve in water. Cells can combine small molecules into large macromolecules, forming a higher level in the biological hierarchy. Macromolecules are polymers, chains of identical or similar subunit molecules called monomers. Although there is a limited number of monomers common to all organisms, each organism is unique because of the specific arrangement of there monomers into polymers with distinctive structures and properties. Monomers of all four classes of macromolecules form larger molecules by a number of different methods for example, dehydration and synthesis, a chemical reaction in which one monomers donates a hydrolysis. In this way large molecules in food are digested into monomers small enough to enter our cells.
The covalent structure of a protein is composed of hundreds of individual bonds. Because free rotation is possible around a good portion of these bonds, there are a very high number of possible conformations the protein can assume. However, each protein is responsible for a particular chemical or structural function, signifying that each one has a distinctive three-dimensional configuration. By the early 1900’s, numerous proteins had been crystallized. Because the ordered collection of molecules in a crystal can only form if all of the molecular units are the same, the discovery that proteins could be crystallized proved that even large proteins have distinct chemical structures. This deduction completely transformed the understanding of proteins and their respective functions. It is important to investigate how a series of amino acids in a polypeptide chain is translated into a three-dimensional protein structure. There are five general topics related to this process: the structure of a protein is determined by its amino acid sequence, the role of a protein is dependent on its unique structure, an isolated protein typically exists in a small number of stable forms, non-covalent interactions are the most important stabilizing forces in a protein structure, and there are structural patterns that aid in explaining and understanding protein architecture.
Initially I struggled to understand that how could such small molecules, like ,dna, proteins and so on carry out such heavy and important functions in our body.
This report provides an insight into the differences in the structure of cells and the way that they carry out their internal mechanisms. Cells form the basis of all living things and they are the smallest single unit of life. Cell biology is the study of cells and how they function, from the subcellular processes which keep them functioning, to the