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How is the structure of proteins related to their functions
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Using appropriate examples and diagrams, describe the primary, secondary, tertiary and quaternary structure of proteins. What molecular forces hold these structures? Proteins are a fundamental macromolecule, playing an essential role in the creation of life, coded for by genes in DNA. Proteins have a wide range of functions in the body, with perhaps the most significant being their role as enzymes. It is these enzymes that are responsible for the biological catalysis of almost all essential cellular reactions that constitute basic life. This range would not be possible without their diversity in structure, as a protein’s structure is directly linked to its functions. Proteins are able to achieve this variety by having a four-tiered structural ‘hierarchy’ with four layers of structure; primary, secondary, tertiary and …show more content…
Horton, R.A. Scrimgeour, G. et al. (2014a) "Amino Acids and the Primary Structure of Proteins" In Principles of Biochemistry: Pearson New International Edition Fifth Edition ed. Edinburgh Gate, Harlow, Essex, CM20 2JE: Pearson Education Limited. pp. 83. Moran, L.A. Horton, R.A. Scrimgeour, G. et al. (2014b) "Amino Acids and the Primary Structures of Proteins" In Principles of Biochemistry: Pearson New International Edition Fifth Edition ed. Edinburgh Gate, Harlow, Essex, CM20 2JE: Pearson Education Limited. pp. 94. Moran, L.A. Horton, R.A. Scrimgeour, G. et al. (2014c) "Proteins: Three-Dimensional Structure and Function" In Principles of Biochemistry: Pearson New International Edition Fifth Edition ed. Edinburgh Gate, Harlow, Essex, CM20 2JE: Pearson Education Limited. pp. 133-134, 135. Richardson, J.S. (2007) The Anatomy and Taxonomy of Protein Structure. [Online]. Available from: http://kinemage.biochem.duke.edu/teaching/anatax/html/anatax.2b.html [Accessed October 2014]. Wu, G., Wu, Z., Dai, Z., et al. (2013) Dietary requirements of "nutritionally non-essential amino acids" by animals and humans. Amino acids, 44 (4):
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).
Conditionally essential amino acids: this are present in many foods, but are not always required to be a part of the daily diet. So long as we successfully absorb sufficient amounts of the essential amino acids, the liver is able to synthesise the remaining others conditionally amino acids. At certain times in life and in certain population groups these amino acids must be supplied by the diet to ensure good health. An adequate intake of the conditionally essential amino acids will also help to spare valuable resources of essential amino acids.
There are nine amino acids that are considered “essential” for health, which we must obtain from our diets since our bodies cannot make them on their own. Some of the roles that amino acids/proteins have include helping to form and maintain muscle mass, providing energy for our cells and brain, helping store away energy for later use in fat stores, making your heart beat, and helping build the foundation of vital organs, including your heart, lungs and even your DNA, and supporting growth/development. Because of its ties to lean muscle mass and satiety in terms of controlling your appetite, protein is especially important as you age.
Due to the nature of amino acids, a titration curve can be employed to identify
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...
On the contrary, plant protein sources, such as beans, lentils and nuts are considered to be incomplete, as they lack one or more of the essential amino acids that your body needs (1).
Each protein is a large complex molecule; these molecules are made up of. of a string of amino acids. There are 20 different amino acids that occur naturally to form proteins and they all have the same basic structure. The. The 20 amino acids the body needs can be linked in.
VMD can be useful to a range of audience, molecular structural data obtained from VMD can be integrated with bioinformatics, which will then provide useful information to researchers of biological system, not only individuals involved with the field of biological science, but also theoretical and experimental researchers of chemical science can utilize the information to scrutinize the chemical structure of molecules. It can also be used in educational institutions to display molecules in a very descriptive manner to students, to give them a broader idea of the structural function.
2. Nelson, David L. and Michael M. Cox. Lehninger Principles of Biochemistry. 3rd ed. Worth
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.
Moderation is vital in all aspects of life and is necessary for overall health, including with one’s food intake. Protein is one of the many important nutrient building blocks that is necessary for proper growth and good health. However, eating excessive amounts of any nutrient or inadequate amounts, can cause various health concerns. Scientists have been able to estimate the amount of nutrients that the body requires. However, the amount of any particular nutrient varies from person to person, depending on your “age, sex, general health status, physical activity level, and use of medications and drugs” (Schiff 2013). It is also important to remember that consuming the required amount of nutrients that meets your dietary guidelines does not