Protein Characteristics and Its Suitability for Polymer Development Proteins are prepared by basic unit called amino acids. The protein’s structure is broadly classified into four major categories which are called primary, secondary, tertiary and quaternary structure. The primary structure of a protein is a linear polymer with a string of amino acids coupled by peptide bonds. Secondary structures of proteins are usually very regular in their conformation and in point of fact, they are the spatial arrangements of primary structures. ‘Alpha Helices’ and ‘Beta Pleated Sheets’ are two types of secondary structures and they are majorly stabilized by hydrogen bonds. The tertiary structure of a protein is the three-dimensional structure and is stabilized by the series of hydrophobic amino acid residues and by disulphide bonds formed among two cysteine amino acid. While the tertiary structure with less disulphide bonds, which form weak, rigid structures that are bendable, but still tough and can oppose rupture such as hair and wool. Structures that contain more disulphide bonds lead to stronger, stiffer and harder structures. Quaternary Structure of protein is the arrangement of two or more chains, to form an entire unit. The interactions between the chains are not dissimilar from those in the tertiary structure, but are distinguished only by being an inter-chain rather than an intra-chain. The quaternary structure involves the clustering of numerous individual peptide chains into an ultimate shape. A range of bonding interactions, including salt bridges, hydrogen bonding, and disulphide bonds hold the a variety of chains into a particular geometry. There are two major categories of proteins with quaternary structure, i.e. fibrous and glo... ... middle of paper ... ...en used as biomaterials in drug delivery systems [36] and in tissue engineering [37]. Scientist reported that the Young’s modulus of rat tail collagen type I vary between 3.7 GPa to 11.5GPa [38]. A series of studies has focused on the structural and tensile properties of collagen scaffolds for the purpose of designing functional biomaterials for clinical application [39-42]. The investigations in a range of proteins such as gluten [43], corn zein [44], soya [45] and milk [46] revealed that these proteins acquire the capability to form films which can be used in food packaging. These proteins have nutritional value as well so it can be used for development of film. In recent duration, the progress of degradable films from protein has drawn attention to a large extent. This is due to protein’s skill to form films and also for its large quantity and renewable nature.
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.
Not all attributes are obvious for every situation. The lion's share of instances of OI (conceivably 85-90 %) are created by a predominant change in a quality coding for sort I collagen (Types I, II, III, and IV in the accompanying rundown). Sorts VII and VIII are recently recognized structures that are acquired in a passive way. The qualities bringing about these two sorts have been recognized. Sorts V and VI don't have a sort 1 collagen change, however the qualities bringing about them have not yet been recognized. The general components of each referred to sort of OI are as per the
It regulates the ratio between epithelial cells and collagen fibers as well as changes in their morphology. The imbalance of collagen metabolism and its arrangement is attributed to many factors which result in increased synthesis of collagen by fibroblasts and myofibroblasts, which in turn inhibit the activity of collagenase, leading to extensive scar hyperplasia. Matrix changes, mainly changes in fibronectin and mucopolysaccharides, result in scar stiffness. MEBO Scar Ointment can accelerate the re-arrangement of twisted collagen andreduce proliferation of fibroblasts, thus restricting scar hyperplasia. [11,13,14,15 ,21] The accumulation and synthesis of mucopolysaccharide can also be reduced once local tissues are compressed, thus reducing generation of collagen and the corresponding scar tissue. [11] Moreover, massaging the MEBO Scar ointment onto old scars can potentially reduce blood supply within scars, decrease synthesis of collagenous fiber, and,reduce α2-M (alpha 2-macroglobulin) globulin of collagenase in serum which facilitates collagenase activity and speeds up disintegration of collagen in old scars,this facility by applying MEBO scar ointment .
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...
These kinds of polymers have both some advantages and disadvantages. Although they are bioactive and biodegradable and provide high comppressive strength, Degradation of such polymers leads to undesired tissue response due to producing acid formation in degradation process. Metallic scaffolds are another method for bone repair and regenaration. They provide high compressive strength and enormous permanent strength. Metallic scaffolds are mainly made of titanium and talium metals. The main disadvantages of metallic scaffolds are not biodegradable and also discharge metal ions. Recent studies in metallic scaffolds mainly focus on biodegradable materials which can be used improve bioactivity of metals such as titanium.
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).
These molecules are identified as globular proteins with a three dimensional structure and are composed of one or more polypeptide chains. The polypeptide chain or chains within an enzyme are folded to form a specific active site. Each different structured active site and only catalyses a certain substrate that fits; this is known as the lock and key model (Cooper, 2000).
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.
Hydrogen bonding- this bonding occurs between the hydrogen and oxygen or nitrogen between amino acids opposite each other. This bond occurs because the oxygen is slightly negative and the nitrogen/hydrogen is slightly positive so there is an attraction between them when they come close together. This is a fairly weak bond however it forms a vital part in helping the structure stay strong and in the right
In its nature, collagen is like the backbone of the skin and is responsible for its elasticity and structure. It’s also responsible for replacement of dead skin cells with new ones giving the skin a radiant
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...
Domains may be considered to be connected units, which are to varying extents independent in terms of their structure, function and folding behaviour. Each domain can be described by its fold. While some proteins consist of a single domain, others consist of several or many. A number of globular protein chains consist of two or three domains appearing as 'lobes'. In other cases the domains may be of very different nature- for example some proteins located in cell membranes have a globular intracellular or extracellular domain distinct from that which spans the membrane.
1443 - 1460. Keener, K., Hoban, T. and Balasubramanian, R. 2014. Biotechnology and its applications. [online] Available at: http://www.ces.ncsu.edu/depts/foodsci/ext/pubs/bioapp.html [Accessed: 11 Apr 2014].
Antimicrobial Packaging: Edible films are produced which incorporate cinnamon, zinc, calcium, oregano oil or other materials that can kill bacteria.