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Structure of proteins related to their function
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Part A: Describe protein structure, the level of structure and geometry. Include in a description of the significance of structure and how it affects to analysis. Protein Structure Levels There are four levels of protein structure which are separated from one another by the degree of complication in the polypeptide chain. A protein molecule can consist of one or more of the protein structure types. 1- ) Primary Structure is the sequence of a chain of amino acids. Proteins are formed from 20 different amino acids. Amino acid are composed of a carbon (α carbon) that bond to the hydrogen atom (H), a carboxyl group (-COOH), an amino group (-NH2) and a variable group, or R group. The primary structure is determined during translation. There are two tools uses to determine the primary structure; Edman degradation and mass spectrometry. Primary structure controls the secondary, tertiary and quaternary structures. It is also used to determine the molecular mass and isoelectric point. 2- )Secondary Structure describes the coiling or folding of a protein due to exclusive hydrogen bonding between its backbone amide and carbonyl groups. These secondary structures are held together by hydrogen bonds. There are three types of secondary structures in proteins. a-) Alpha helix (α-helix) is a spiral arrangement around polypeptide backbone. The inner part of the coil is formed by the backbone of the peptide while the side chains extend outward from the coil. Hydrogen bonds between N-H of one amino acid and the C=O on the 4th amino acid stabilize the helix. b-) Beta pleated the beta sheet involves H bonding between the backbone residues in adjacent chains. The orientation of a beta pleated sheet can occur in two types. The strands may be paralle... ... middle of paper ... ...Da) than grw175 (28 kDa) proving that the above observation is true. b-) Molecular mass of the XøD2788 gene product = 56 kDa 1.) Loaded the image of the gel into ImageJ 2.) Labeled the MW ladder lane then other lanes of interest (lane 2 grw175, lane 3 grw19) 3.) A graph representation was then generated 4.) I selected the peaks of MW lane to be used in the molwt.macros program 5.) Based on the calculations that were generated using the molwt macros program I was then able to select the peaks of interest and compute a numerical value for them 6.) ImageJ indicated a peak of 56kda for grw19 positive and a 28kda value in grw175 positive. 7.) Using the numerical values I was able to subtract the grw175 estimated size of 28kda from the size of what is believed to be the fusion protein grw19 56kda 8.) Grw175 = 28kda – fusion protein 56kda to give you a value of = 28kda
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 ... ...
UV-254 nm, 15 V, 60 Hz, 0.16 A). Masses were taken on a Mettler AE 100. Rotary
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.
contains three components. First it is constructed with a phosphorylated head group, then a three
Accuracy: This paper demonstrates much accuracy, this is proven through the subtitles, statistics and in text citations for
Proteins are one of the main building blocks of the body. They are required for the structure, function, and regulation of the body’s tissues and organs. Even smaller units create proteins; these are called amino acids. There are twenty different types of amino acids, and all twenty are configured in many different chains and sequences, producing differing protein structures and functions. An enzyme is a specialized protein that participates in chemical reactions where they serve as catalysts to speed up said reactions, or reduce the energy of activation, noted as Ea (Mader & Windelspecht).
Abstract/Summary: “Proteins account for more than 50% of the dry weight of most cells, and they are instrumental in almost everything organisms do” (Campbell, 1999). The significance of proteins to the continuation of our biological systems is undeniable, and a study of how to quantify proteins seems an appropriate introduction to our studies of biology. In order to study proteins we must first know how to separate then quantify the amount using basic principles of experimental design such as a standard curve. In this experiment we wish to quantify the amount of previously extracted protein by measuring the absorbance of the unknown amount and determining its concentration by overlaying it against a standard curve of the absorbance of known concentrations of the protein. We used the dye agent Bradford Protein Assay to get an absorbance of 0.078, 0.143, 0.393, 0.473, and 0.527 at the protein’s respective concentrations of 0.28, 0.56, 0.84, 1.12, and 1.40 mg/mL. When a best-fit line was applied to the standard curve, and the absorbance of our unknown concentration (0.317 A) plotted, we estimated a concentration of around 0.84 mg/mL of protein. Our calculations indicated a quantity of 168 mg of protein, which was an approximately 8.96% yield of the projected 1875 mg that was expected. Errors that may have led to this small yield percentage may have stemmed from our previous lab and our initial attempts to extract the desired amount of protein.
...Hallert, C., C. Grant, S. Grehn, C. Grannot, S. Hultent, G. Midhagens M. Strom, H. Svensson,
n.d. - n.d. - n.d. Retrieved from http://www.dd-692.com/atomic.htm.
Due to the nature of amino acids, a titration curve can be employed to identify
Zhang, Y. B., Harwood, J., Williams, A., Ylänne-McEwen, V., Wadleigh, P. M., & Thimm, C.
Schreuder, Jolanda A. H.; Roelen, Corné A. M.; van Zweeden, Nely F.; Jongsma, Dianne; van der Klink, Jac J. L.; Groothoff, Johan W.
Protein domains occur in large polypeptides, (proteins that have more than 200 residues). These proteins have two or more globular clusters which in turn have domains composed of 100-200 amino acids. Thus many domains are structurally independent units that have the characteristics of small globular proteins.
Proteins are considered to be the most versatile macromolecules in a living system. This is because they serve crucial functions in all biological processes. Proteins are linear polymers, and they are made up of monomer units that are called amino acids. The sequence of the amino acids linked together is referred to as the primary structure. A protein will spontaneously fold up into a 3D shape caused by the hydrogen bonding of amino acids near each other. This 3D structure is determined by the sequence of the amino acids. The 3D structure is referred to as the secondary structure. There is also a tertiary structure, which is formed by the long-range interactions of the amino acids. Protein function is directly dependent on this 3D structure.
A peptide is a chemical compound consisting of two or more amino acids that are joined by a peptide bond. This bond is a unique connection in which the nitrogen atom of one amino acid binds to the carboxyl carbon atom of another.