Could computer-designed drugs target deadly diseases? Drugs are medicines or substances that affect the way in which the body works. Salt is dissolved in water to speed us corrosion and in a similar way enzymes (proteins) act as biological catalysts to speed up chemical reactions in the body. All cells in the body have proteins knowing that cells come in different sizes and shapes including its cytoplasm which consists of ribosome needed for proteins. Disease-causing cells need to be dealt with drugs in order to avoid development. In terms of targeting diseases, the drug binds with the enzyme according to its charges and shape. The process of drugs targeting deadly diseases is also known as the ‘lock and key’ modelling, however it does not necessarily symbolize the process (I will analyse this theory later on). Computer-designed drugs involve the visualisation and mapping of molecules intended to bind with proteins with the purpose of destroying them. Computer-designed drugs are an advantage in the sense of being able to have a 3D model showing the different elements to it; conversely some people may think that it is a complex process so scientists can simply use trial and error instead. Consequently we have had debates over time about whether computer-designed drugs are actually a help and would it target deadly diseases and not just harmless diseases. In this essay I will be addressing whether computer-designed drugs will target deadly diseases with the help of different technical approaches to how it works. As we all probably should know, proteins are the building blocks of life and when you look at someone, you are scientifically looking at their proteins which include their skin, eyes and so on. This implies that there a... ... middle of paper ... ...d to water) then it would try to move to the outer part of the sequence and conversely hydrophobic amino acids would try to move to the inner part of the sequence. After this stage, the quaternary structure comes along which is when two or more polypeptides are put together and form more complex structure with their relationship with water molecules and their charges. Polypeptides become proteins at this stage and haemoglobin is an example of a quaternary protein structure. This is so that it has a larger area to take lots of oxygen for transportation. Works Cited [1] http://uk.ask.com/wiki/Protein [2] http://www.livestrong.com/article/531152-5-elements-of-protein/ Figure 1: http://education-portal.com/academy/lesson/what-are-amino-acids-definition-structure-quiz.html#lesson Figure 2: http://blog.science-matters.org/2012/10/08/biomolecules-protein-structure/
The shape of the protein chains that produce the building blocks and other structures used in life is mostly determined by weak chemical bonds that are easily broken and remade. These chains can shorten, lengthen, and change shape in response to the input or withdrawal of energy. The changes in the chains alter the shape of the protein and can also alter its function or cause it to become either active or inactive. The ATP molecule can bond to one part of a... ... middle of paper ... ...
The primary structure is the sequence of amino acids that make up a polypeptide chain. 20 different amino acids are found in proteins. The exact order of the amino acids in a specific protein is the primary sequence for that protein. [IMAGE] [IMAGE]Protein secondary structure refers to regular, repeated patterns of folding of the protein backbone. The two most common folding patterns are the alpha helix and the beta sheet.
Pharmaceuticals have examined and found to ”work by changing the biological functions of the target cells in the body through chemical agents“ (Doweiko, 2015, p. 16). ”Many people in the past have thought that drugs that
Zhang X., Tang H., Ye C. and Liu M. (2006). Structure-based drug design: NMR-based approach for ligand-protein interactions. Drug Discovery Today: Technologies. 3 (3), pp. 241-245.
Eyesenkes theory provides an amicable solution. If we could assume that this information was genetically coded in to the cells at birth then this no longer becomes an issue and we can explain how’s and why the constructs are laid down to a loose genetic template i.
1. "Dangerous Designer Drug Packs a One-two Punch." - VCU Center for Clinical and Translational Research. N.p., n.d. Web. 22 Nov. 2013
Engel, G. L. (1977). The need for a new medical model: a challenge for biomedicine. Science, 196(4286), 129–136.
I would like to thank Salish Kootenai College for giving me the wonderful opportunity of applying for STEM academy. If somebody had told me that I would be applying for college classes as a sophomore, I would not have believed them. My parents have always told me that when an opportunity comes, you should take it, and I do not plan on letting this experience go to waste. Education has been a big part of my life, and this academy can only help me move forward. That being said, here are a few reasons why I should be considered a candidate for the STEM academy. Joining the STEM academy will allow me to further my knowledge and help me to get closer to my goals, my academic career would flourish, and I would be closer to my ambition for my future. I am determined to become the best and most educated version of myself that I can possibly be.
A three-dimensional structure of hemoglobin is determined by X-ray crystallography showed hemoglobin is made up of four polypeptide chains, each of those chains has a very similar three-dimensional structure to the single polypeptide chain in myoglobin. The major type of hemoglobin found in adults (HbA) is made up of two different polypeptide chains: the alpha-chain that consists of 141 amino acids residues, and the beta-chain of 146 residues. Each chain, like that in myoglobin consist of eight alpha-helices and each contains a heme prosthetic group. Therefore, hemoglobin can bind four molecules of oxygen. The four polypeptide chains, two alpha and teo beta, are packed tightly together in a tetrahedral array to form an overall spherically shaped molecule that is held together by multiple noncovalent interactions.
Following Baum’s reasoning, the Biomedical Model is centred upon the treatment of health problems. For example if a person has a disease or falls ill the Biomedical Model’s focus is towards the body’s physical processes, which includes biochemical, pathological and physiological (Fanany, 2012). This diagnostic approach involves firstly, locating the cause of the illness (the pathogen), and secondly, treating the illness accordingly using Westernised medical interventions (such as drugs or surgery).
Over the past decade, scientists have made significant advancements in the treatment of certain diseases. Unfortunately, just like any new product, the cost of developing these new technologies and treatments is extremely high. Plus, unlike other technology, heath technolo...
n.d. - n.d. Peptides and Proteins. Proteins. Retrieved July 25, 2008, from http://www.cd http://www.cem.msu.edu/reusch/VirtualText/protein2.htm Ophardt, C. E. (2003).
An inspection of the modern animal phyla will reveal that eyes are just as diverse as they are complex. Some organisms like the rag worm have pigmented cup eyes while other like he box jellyfish have two lens eyes and two pairs of pigment pit eyes. To account for the diversity in eye structure, we must first examine the eye ‘prototype’, the original structure that was acted upon by evolution. The simplest organ that can be considered an eye is composed of a single photoreceptor cell and a single pigment cell, without any lens or other refractive body (Arendt, 2003). Such organs are know as eyespots, and...
Proteins are considered to be the most versatile macromolecules in a living system. This is because they serve crucial functions in all biological processes. Proteins are linear polymers, and they are made up of monomer units that are called amino acids. The sequence of the amino acids linked together is referred to as the primary structure. A protein will spontaneously fold up into a 3D shape caused by the hydrogen bonding of amino acids near each other. This 3D structure is determined by the sequence of the amino acids. The 3D structure is referred to as the secondary structure. There is also a tertiary structure, which is formed by the long-range interactions of the amino acids. Protein function is directly dependent on this 3D structure.
In the hierarchial organisation of proteins, domains are found at the highest level of tertiary structure. Since the term was first used by Wetlaufer (1973) a number of definitions exist reflecting author bias, however all of the definitions agree that domains are independently folding compact units. Domains are frequently coded by exons and therefore have specific functionality. Among the many descriptions of protein domains the two most striking and simple are " Protein evolutionary units" and "Basic currency of Proteins".