Myoglobin

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Submitted By markaw91
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Myoglobin is an extremely compact heme protein (MW ~ 17 800), found primarily in cardiac and red skeletal muscles. It functions in the storage of oxygen and facilitates the transport of oxygen to the mitochondria for oxidative phosphorylation. Myoglobin consists of a single polypeptide chain of about 153 amino acids and approximately 1200 atoms (excluding hydrogen). Approximately 70% of the main chain is folded into eight major, right-handed a -helices. The majority of the rest of the chain forms turns between helices devoid of symmetry. [1]
Protein stability is caused the non-covalent bonds that keep the secondary, tertiary and quaternary structures of a protein intact. Denaturants such as Guanidinium-HCL disrupt these covalent bonds and cause the protein to unfold and lose its secondary and tertiary structures but without break the peptide covalent bonds between the amino acids.
Circular Dichroism (CD) is a spectroscopic technique widely used for the evaluation of the conformation and stability of proteins in several environmental conditions like temperature, ionic strength, and presence of solutes or small molecules. Circular dichroism (CD) spectroscopy measures differences in the absorption of left-handed polarized light versus right-handed polarized light which arise due to structural asymmetry. The absence of regular structure results in zero CD intensity, while an ordered structure results in a spectrum which can contain both positive and negative signals. CD probes the secondary structure of proteins because the peptide bond is asymmetric and molecules without a plan of symmetry show the phenomenon of circular dichroism. [2]

Myoglobin is an extremely compact heme protein (MW ~ 17 800), found primarily in cardiac and red skeletal muscles. It functions in the storage of oxygen and facilitates the transport of oxygen to the mitochondria for oxidative…...

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