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The function and structure of proteins essay
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The function and structure of proteins essay
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Hierarchical Structure of Proteins Molecular Cell Biology. 4th edition, Dec 18th, U.S. National Library of Medicine, This article intends to educate the reader on how exactly proteins function and their structure and how the various components of proteins work together to create one cohesive unit. This passage focuses on the spatial arrangement of proteins emphasizing its importance as key to understanding how exactly proteins work. In summary, this excerpt went over how proteins are a linear polymer of amino acids linked together by peptide bonds. There are various interactions between the amino acids, which are mostly non-covalent, that stabilize the structure of a folded protein. There are 20 unique amino acids found naturally and can be grouped into three categories based off the nature of their R groups located on the side of the amino acids. Hydrophilic, hydrophobic or amino acids with a special R group which are composed of cysteine, glycine and proline. The Alpha helix and beta sheet are the most abundant structures of protein secondary structures. These stabilize hydrogen bonds between atoms and thus the protein …show more content…
It talks about protein structure and goes into detail about its structure emphasizing that its spatial arrangement is key to understanding how proteins work. This information would be most relevant to students studying this topic or people in biotechnology fields manufacturing the next vaccine for some kind of disease. This information would be useful in aiding vaccine development because to create a vaccine through chemical synthesis, scientists must isolate a gene which encodes for an antigen and then find the sequence of amino acids which make up that antigen. Once that is done scientists can assemble a protein molecule chemical by chemical making a wholly synthetic protein to help fight against the
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 ... ...
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).
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.
Wissmueller S., Font J., Liew C.W., Cram E., Schroeder T., Turner J., Crossley M., Mackay J.P. and Matthews J.M. (2011). Protein-protein interactions: analysis of a false positive GST pulldown result. Proteins. 79 (8), pp. 2365-2371.
Proteins are one of the main building blocks of the body. They are required for the structure, function, and regulation of the body’s tissues and organs. Even smaller units create proteins; these are called amino acids. There are twenty different types of amino acids, and all twenty are configured in many different chains and sequences, producing differing protein structures and functions. An enzyme is a specialized protein that participates in chemical reactions where they serve as catalysts to speed up said reactions, or reduce the energy of activation, noted as Ea (Mader & Windelspecht).
The Structure and Function of Carbohydrates Large biological molecules are called macromolecules, there are giant molecules (polymers) made up of repeating units (monomers). Carbohydrates are one of the main classes of biological molecules. Macromolecule units (monomers) are joined together by condensation reactions and hydrolysis reactions split macromolecules down into their individual units. Carbohydrates are molecules that contain elements of carbon, hydrogen, and oxygen. Carbohydrates have a 2:1 hydrogen to oxygen ratio, there are twice as many hydrogen atoms as oxygen atoms (the same proportion as in water).
Protein have connection with amino acid to help in functions of: skin, muscle, hair and bones
Prion proteins are small infectious particles that are formed by the miss-folding of the protein structure. It is believed the miss-folding of such proteins has been the cause of disease such as Bovine spongiform encephalopathy in cows and Creutzfeldt-Jakob disease in humans. The prion proteins that are known to mankind so far suggest that they affect the brain of the affected individual. “A study1 in the British Medical Journal reveals that 1 in 2,000 people in the United Kingdom might harbour the infectious prion protein that causes variant Creutzfeldt–Jakob disease (vCJD).”(Callaway, 2013). The study therefore shows that a high number of people are at risk and this is a cause for concern as the prion protein which is miss-folded prompts normal proteins present in the brain, to alter their structure so they also become miss folded. The miss folded structure is understood to be very stable and as levels of the protein build up within the infected tissue this results in destruction and eventually death of the cell. The prion protein, PrP is thought to be the cause of all mammalian prion diseases but the structure of the protein is yet to be discovered. The normal cellular form of the prion protein is PrPc, whereas the miss folded scrapie form is PrPSc. PrPc is constructed from 209 amino acids and one disulphide bond and are found on cell membranes. “Several topological forms exist; one cell surface form anchored via glycolipid and two transmembrane forms.”(Hedge et al, 1998). The miss folded form, PrPSc has more Beta sheets however the normal form PrPc has Alpha structure present. “Fourier-transform infrared (FTIR) spectroscopy demonstrated that PrPC has a high alpha-helix content (42%) and no beta-sheet (3%), findings that were c...
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).
Sequence and structural proteomics involve the large scale analysis of protein structure. Comparison among the sequence and structure of the protein enable the identification on the function of newly discovered genes (Proteoconsult, n.d.). It consists of two parallel goals which one of the goals is to determine three-dimensional structures of proteins. Determine the structure of the protein help to modeled many other structures by using computational techniques (Christendat et al., 2000). This approach is useful in phylogenetic distribution of folds and structural features of proteins (Christendat et al., 2000). Nuclear magnetic resonance (NMR) spectroscopy is one of the techniques that provide experimental data for those initiatives. It is best applied to proteins which are smaller than 250 amino acids (Yee et al., 2001). Although it is limited by size constraints and also lengthy data collection and analysis time, it is still recommended as it can deliver strong results. There are two types of NMR which are one-dimensional NMR and two-dimensional NMR. One-dimensional NMR provides enough information for assessing the folding properties of proteins (Rehm, Huber & Holak, 2002). It also helps to identify a mixture of folded and unfolded protein by observing both signal dispersion and prominent peak. Observation in one-dimensional spectrum also obtains information on molecular weight and aggregation of molecule under investigation. In spite of this, two-dimensional NMR are used for screening that reveal structural include binding, properties of proteins. It also provides important information for optimizing conditions for protein constructs that are amenable to structural studies (Rehm et al., 2002). NMR is a powerful tool which it w...
thousands of different ways to form thousands of different proteins. each with a unique function in the body. Both the amino acids manufactured in the liver and those derived from the breakdown of the The proteins we eat are absorbed into the blood stream and taken up by the cells and tissues to build new proteins as needed.... ... middle of paper ... ...denatured by boiling, their chains are shortened to form gelatine.
"Within a single subunit [polypeptide chain], contiguous portions of the polypeptide chain frequently fold into compact, local semi-independent units called domains." - Richardson, 1981
There are four main levels of a protein, which make up its native conformation. The first level, primary structure, is just the basic order of all the amino acids. The amino acids are held together by strong peptide bonds. The next level of protein organization is the secondary structure. This is where the primary structure is repeated folded so that it takes up less space. There are two types of folding, the first of which is beta-pleated sheets, where the primary structure would resemble continuous spikes forming a horizontal strip. The seco...
To compose a protein, cells have to set a series of amino acids collectively in the right sort. initial, it make a duplicate of the relevant DNA order in the cell nucleus, and take it into the cytoplasm - a spot like make a copy of the instruction booklet since the manager place of work out to the gathering ranks in a car factory. At this point, the cells decode the order and make a lot of protein copies, which fold into form as they are
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.