Denaturing of proteins
Denaturing of Proteins Research Paper
Abstract:
Introduction
The experiments the objective is to determine, the possible measures of the denaturation process of several proteins by using a home based temperate The necessary applications of this experiment are to compile all the possible measures of the denaturation process in understandable units and explainable means. Other methods possible for research are by using a method that was used in this experiment is scientifically logical due to the fact that it can be done easily and at a low cost while producing sound and replicable data. All in all the experiment is able to produce data that is obtained simplistically while being applicable to the scientific community. The process of denaturation is very simple when carried out skillfully and carefully. When a solution of a protein is boiled, the protein frequently becomes insoluble—i.e., it is denatured—and remains insoluble even when the solution is cooled. The denatured protein has the same primary structure as the original, or native, protein. The weak forces between charged groups and the weaker forces of mutual attraction of nonpolar groups are disrupted at elevated temperatures, however; as a result, the tertiary structure of the protein is lost. In some instances the original structure of the protein can be regenerated; the process is called renaturation. (Haurowitz Felix, 2013)
Changing the conformation of a protein either temporarily or permanently by disrupting these forces is called denaturation. Denaturation results in a loss of activity. Since the native conformation is usually the most water soluble, disrupting the secondary and tertiary structures causes changes in solubility and frequently results in precipitation of the protein from solution. Reagents or conditions that can cause denaturation are called denaturing agents; these include heat, pH
Abstract:
Introduction
The experiments the objective is to determine, the possible measures of the denaturation process of several proteins by using a home based temperate The necessary applications of this experiment are to compile all the possible measures of the denaturation process in understandable units and explainable means. Other methods possible for research are by using a method that was used in this experiment is scientifically logical due to the fact that it can be done easily and at a low cost while producing sound and replicable data. All in all the experiment is able to produce data that is obtained simplistically while being applicable to the scientific community. The process of denaturation is very simple when carried out skillfully and carefully. When a solution of a protein is boiled, the protein frequently becomes insoluble—i.e., it is denatured—and remains insoluble even when the solution is cooled. The denatured protein has the same primary structure as the original, or native, protein. The weak forces between charged groups and the weaker forces of mutual attraction of nonpolar groups are disrupted at elevated temperatures, however; as a result, the tertiary structure of the protein is lost. In some instances the original structure of the protein can be regenerated; the process is called renaturation. (Haurowitz Felix, 2013)
Changing the conformation of a protein either temporarily or permanently by disrupting these forces is called denaturation. Denaturation results in a loss of activity. Since the native conformation is usually the most water soluble, disrupting the secondary and tertiary structures causes changes in solubility and frequently results in precipitation of the protein from solution. Reagents or conditions that can cause denaturation are called denaturing agents; these include heat, pH
References: 1. Millett IS, Doniach S, Plaxco KW. Toward a taxonomy of the denatured state: small angle scattering studies of unfolded proteins. Protein Fold. Cell. 2002;62:241–262. [PubMed] 2. Uversky VN. Natively unfolded proteins: a point where biology waits for physics. Protein Sci.2002;11:739–756. [PMC free article] [PubMed] 3. Fleming PJ, Rose GD. Conformational properties of denatured proteins. In: Buchner J, Kiefhaber T, editors. Protein Folding Handbook. Part 1. Vol. 2. 2005. pp. 710–736.