The Atomic Cloud and Model of Hemoglobin Structure
The red blood cells in both animal and human blood are made up of several materials. Key among them includes the red blood cells and other cells within the fluid that flows all through the body carrying both oxygen and nutrients. Red blood cells are known to be produced by one of the bone marrows, and perform the function of transport of oxygen from one part of the body to the other; one notable aspect of these cells is that the large percentage of their internal structure is composed of the protein haemoglobin. The role of haemoglobin illuminates the main function of the cells based on their structure and properties. The reason why it is possible for haemoglobin to transport oxygen to the rest of the body is anchored on its affinity to the beneficial gas. Known as being hexagonal or rhombic in nature, research has found haemoglobin to be crystalline in nature and its existence as an entity containing iron element affiliated parts makes it suitable for its function. Thus, in the process of performing an X-ray crystallography, the first step is to segregate the haemoglobin from other components of the cell. This requires the processes of cell disruption in order to open up the cell membrane, an action which in turn releases the components of the cell into a liquid medium (Mielczarek, 1993).
Processes, such as centrifugation and various rotation rates per unit time will ensure the separation of the haemoglobin protein from other components of the disrupted red blood cell. Upon separation, the remaining haemoglobin containing solution gives can be purified through processes, such as evaporation in order to remain with the specified crystals of the protein. This step paves way for the performance of X-ray crystallography in a bid to view the physical structure of the protein. Apparently, the crystalline nature of these structures comes about as result of their water component aspect. The first precaution in crystallography is to keep them in the crystalline form by retaining the water. Thus, they are placed on wet glass capillaries, followed by illumination of a single crystal by a relatively narrow beam of X-ray. In order to view the three-dimensional structure of the protein, the crystal is rotated gently within the path of the beam. The photographic film on the other side of the beam records the information in form of dots or spot. Each spot is interpreted to give information on the structural arrangements of the atoms, and gives the avenue to create a lattice structure (Mielczarek, 1993).
Scientific investigative methods have strong points they can explain as facts. Not all aspects of a study can be explained by the use of a single method. X-ray crystallography in the experiment, for example, gives the dimension of the crystalline structures as pertain the arrangements of atoms. However, it is not possible to know what specific amino acids constitute the crystals with the same process. In the images of the structures, the difference in the orientation of the CD bend on the alpha and beta structures cannot be understood unless a different method is used. On the other hand, the use of sequencing allows for the knowledge of the arrangement of amino acid backbones to be explained. These sequences have gaps within them that can only be explained using the crystalline structure obtained from the Crystallography. Therefore, the corroborative method as well as the use of control experiment with Myoglobin gives confirmatory results for accurate conclusions to be made (Fasman, 1989).
The structure of proline makes it a unique amino acid because of the way it attaches to the protein backbone. Unlike the other aliphatic amino acids, proline is able to attach to the amino acid backbone more than ones. This makes it most suitable for the formation of bends and turns within the crystalline structures. The straight chains show the orientation that indicates the presence of tryptophan (Mielczarek, 1993). During the formation of the protein, it is worth noting that amino acids come together to form the backbone of the polypeptide chain. This is because in very amino acid, there are the amino group and the carboxylic group, each of which comprise negative and positive portions. For this reason, interactions between the acids will bring about the basic structures and functional properties. They are known as the basic structural components of various tissues that form organs and organ systems. On the other hand, they also bear functional aspect as the various functions of providing basic components of supporting structures, hormonal interactions, as well as immune-related roles. It is with these in mind that the study of specific proteins, their structure, and the resulting functional properties become an important portion of scientific study.
In addition, it is worth noting that as the amino acids come together in this process, the bonds between the two sides of each amino acid comes in together with its amino acid side chain. These side chains have different types of chemical compositions and structures. The result of this will lead to different reactions and folding methods, depending on the environments and conditions within the surrounding. This, therefore, means that it is not common to find a protein which has a straight side chain in its tertiary structure. Generally, the side chains of the polypeptide chains will assume a particular shape other than straight. Thus, the appearance in the X-ray diagram shows the reader that it is an impression of the predictability of the shape of the tertiary form of the protein.
Fasman, G. D. (1989). Prediction of protein structure and the principles of protein conformation. New York: Plenum Press
Mielczarek, E. V. (1993). Biological physics. New York: American Inst. of Phy