Protein: Summary
TITLE: The Amount of Protein in Chicken Tissues over Cooked Various Periods of Time.
ABSTRACT: In this lab, we are using a BioRad protein assay dye to determine the concentration of protein in our chicken. The dye binds to the amino acid residues, which allow us to find the concentration of protein (BioRad Protein Assay for Tissues). Our hypothesis was the longer chicken is cooked the less protein is available. To test our hypothesis, we made samples using our chicken and distilled water to determine how much protein was in the chicken. We found that our data supported our hypothesis; it showed that the longer our chicken was cooked the less protein that was in the chicken. As the chicken is cooked longer, the protein is denatured by the heat.
INTRODUCTION: The three dimensional shape of a protein is critical to its function. A protein consists of one or more chains of amino acids that fold into shapes held in place by chemical bonds. The bonds linking the amino acids in a chain are strong, covalent bonds. However, most of the bonds that maintain the three-dimensional shape of proteins are weak bonds- typically hydrogen bonds- that can be broken easily by chemicals or heat (http://www.sumanasinc.com/webcontent/animations/content/proteinstructure.html).Our hypothesis that we are testing is the longer that you cook chicken the less protein that will be in the chicken. We used pieces of chicken cooked at 15, 30, 45, and 60 seconds and also a raw piece as our samples. We will crush our chicken mixed with water in order to create samples that we can use to test the absorbency. We placed the distilled water and chicken samples into small tubes that could be placed in the spectrophotometer in order to get the absorbency reading. We got the readings and recorded the data in order to determine whether our hypothesis was supported.
MATERIALS and METHODS: We adjusted the wavelength on the spectrophotometer to A595 (Lab instructions). We blanked the machine using a tube
ABSTRACT: In this lab, we are using a BioRad protein assay dye to determine the concentration of protein in our chicken. The dye binds to the amino acid residues, which allow us to find the concentration of protein (BioRad Protein Assay for Tissues). Our hypothesis was the longer chicken is cooked the less protein is available. To test our hypothesis, we made samples using our chicken and distilled water to determine how much protein was in the chicken. We found that our data supported our hypothesis; it showed that the longer our chicken was cooked the less protein that was in the chicken. As the chicken is cooked longer, the protein is denatured by the heat.
INTRODUCTION: The three dimensional shape of a protein is critical to its function. A protein consists of one or more chains of amino acids that fold into shapes held in place by chemical bonds. The bonds linking the amino acids in a chain are strong, covalent bonds. However, most of the bonds that maintain the three-dimensional shape of proteins are weak bonds- typically hydrogen bonds- that can be broken easily by chemicals or heat (http://www.sumanasinc.com/webcontent/animations/content/proteinstructure.html).Our hypothesis that we are testing is the longer that you cook chicken the less protein that will be in the chicken. We used pieces of chicken cooked at 15, 30, 45, and 60 seconds and also a raw piece as our samples. We will crush our chicken mixed with water in order to create samples that we can use to test the absorbency. We placed the distilled water and chicken samples into small tubes that could be placed in the spectrophotometer in order to get the absorbency reading. We got the readings and recorded the data in order to determine whether our hypothesis was supported.
MATERIALS and METHODS: We adjusted the wavelength on the spectrophotometer to A595 (Lab instructions). We blanked the machine using a tube
References: Group discussions Lab instructions BioRad Protein Assay for Tissues http://www.sumanasinc.com/webcontent/animations/content/proteinstructure.html arjournals.annualreviews.org/doi/abs/10.1146/annurev.pp.29.060178.000325