2365 Comparative Biochemistry TITLE: Proteins and Amino Acids RESULTS: Table 1: The results of experiment 1; the Lowry Test Volume of Standard Protein/ Unknown (mL) Absorbance at 750 nm 0 0.000 0.1 0.017 0.3 0.135 0.3 0.155 0.5 0.230 0.7 0.323 0.7 0.310 1.0 0.457 1.0 Unknown 1a 0.463 1.0 Unknown 1b 0.433 1.0 Unknown 2a 0.237 1.0 Unknown 2b 0.159 Table 2: The results of Experiment 2; Ninhydrin Test Amino acid Color X Bright yellow Y Dark yellow Z Light
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denotes the necessary shape of the complementary molecule. This is easier explained through an example. An example of a polymer‚ is a protein. The monomer used to make up is an amino acid. When two amino acids join together a dipeptide is formed‚ this is then made into a polypeptide chain by the joining of additional amino acids‚ it finally becomes a protein when more than one of these polypeptide chains link to one another in a condensation reaction. Proteins have a variety of functions‚ these functions
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lab was to find the differences in hemoglobin of gorillas‚ horses‚ and humans Tables: Organism Number of Differences Horse and Gorilla 27 Horse and Human 25 Human and Gorilla 1 Amino Acid Abbreviation Human Gorilla Horse Alanine Ala 14 14 15 Arginine Arg 3 2 4 Aspartic Acid Asp 13 13 14 Cytesine Cys 2 2 1 Glutamic Acid Glu 11 11 13 Glycine Gly 12 13 14 Histidine His 8 8 8 Leucine Leu 17 19 19 Lysine Lys 11 11 11 Methionine Met 1 1 1 Phenylolanine Phe 8 8 8 Proline Pro 7 7 5 Serine Ser 5 5 6 Threonine
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are linear chains of amino acids‚ and there are 20 amino acids found in proteins. So the real question becomes: how does a four letter alphabet code for all possible combinations of 20 amino acids? By constructing multi-letter "words" out of the four letters in the alphabet‚ it is possible to code for all of the amino acids. Specifically‚ it is possible to make 64 different three letter words from just the four letters of the genetic alphabet‚ which covers the 20 amino acids easily. This kind of
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enzyme‚ acts as a catalyst‚ speeding up chemical reactions in the cell. All proteins are composed of the same set of 20 amino acids‚ and each amino acid differs from the other only by the "R group" attached to it. The polymers of those amino acids are called polypeptides‚ and the order of amino acids is vital to the function of the protein. For example‚ if just one amino acid is substituted for another in the primary structure of hemoglobin‚ the protein that carries oxygen in a red blood cell‚
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Coomassie dye only interacts with certain amino acids such as: arginine‚ histidine‚ lysine‚ tyrosine‚ tryptophan and phenylalanine. However‚ each amino acid has different structure from each other; therefore the Coomassie dye will interact differently with each amino acid. The Coomassie dye molecules are bound to proteins by elctronstatic attraction enhanced by hydrophobic bonding (Tal et al. 1984). Besides the interaction between Coomassie dye and amino acids‚ some compounds can interfere the result
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From my diagram I can observe the quaternary structure is 3 helical polypeptides which are looped around and is held by hydrogen bonds. The 3 stranded molecules runs parallel to others and the disulphide cross-linkages between the r-groups of the amino acid holds the molecules together forming fibres. Collagen molecules forms covalent bonds which are called cross links‚ with other collagen molecules next to it. The cross-links that form are shocked along the collagen molecules and adding to the strength
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of as different amino acids joined by peptide bonds. A protein is formed by amino acids which are the basic building block of a protein components of an amino acid include a :C-carbon atom‚ H-Hydrogen atom‚ H3N+ - Amino Group‚ COOH- - Carboxyl Group‚ R- this group varies from amino acid to amino acid. There are 20 amino acids‚ each differing in its R group. Two examples are: Glycine‚ its R group being H(Hydrogen) and Phenylalanine its R group being CH2 (Carbon Hydrogen). Amino Acids are joined together
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is referred to as oxyhemoglobin. Oxyhemoglobin is an unstable protein that easily reverses its’ oxygen attachments. When a molecule of hemoglobin is empty of oxygen attachments‚ it is called deoxyhemoglobin. Portions of the terminal end of the amino acids in the deoxyhemoglobin will work together to form ionic pairs. Tuesday‚ March 12‚ 13 These ionic pairs decrease the acidity of the blood by binding one hydrogen atom for every 2 oxygen molecules released. The resulting lowering of blood pH will
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Campbell’s Biology‚ 9e (Reece et al.) Chapter 5 The Structure and Function of Large Biological Molecules In Chapter 5‚ the principles of chemistry covered in earlier chapters are applied to the understanding of biological polymers and lipid membranes. The emphasis is on properly linking monomers and their polymers‚ and on the structural and functional diversity of the different polymer types. Particular attention is given to protein structure‚ because this is central to understanding subsequent
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