Alpha helix

scorpion can be found in Israel. Chlorotoxin is comprised of 36 amino acids, which make up a small peptide. This polypeptide contains four disulfide bonds and eight cystines. But chlorotoxin has a secondary form that is made up of 3 beta sheets and an alpha helix. Many have been studying the effects that chlorotoxin has on cancer cells. Some of the ingredients that make up the scorpion venom are histamine, serotonin, histamine releasing factors, bio-polysaccharides and protease inhibitors. This…

defining feature is a DNA binding domain known as the fork head domain (Lai et al 1993). This domain is a hundred amino acids long and is highly conserved. It consists of three alpha helices and two large loop regions. The resulting structure resembles butterfly wings and the FOX proteins are sometime refer to as winged helix proteins(Clark et al 1993).…

polymer found in a large variety of foods. Starch is linked by the glucosidic bonds known as alpha-1,4 and alpha- 1,6 (Wang). These linkages and the angles between the carbons allow for Starch to coil into a helix. Starch is primarily used as an energy storing compound in plants. It has two primary forms: amylose and amylopectin. Amylose has primarily a structure of unbranched helices. It is made up of only alpha-1,4 glycosidic linkages (Freeman). Amylose is a polymer with 500 to 2000 of the…

Linus Carl Pauling, an American chemist and biochemist, was many things including an peace activist, educator, and author. Pauling was born on February 28th,1901 in Portland, Oregon to Herman and Lucy Pauling. His father was a pharmacist and his mother was the daughter of one. After his birth the Pauling family moved to Condon, a nearby town. As a child, Linus was a very bright kid. Unfortunately, soon Pauling lost his father to ulcer and as a result of that, his family, which included of him,…

have a wide range of cellular consequences and I will discuss how the activation of rhodopsin, sphingosine-1-phosphate receptors, and beta-adrenergic receptors, can result in these diverse range of consequences. GPCRs are composed of 7 transmembrane alpha helices, connected by 6 hydrophilic loops. There is a large amount of sequence variation amongst GPCR in cytoplasmic loop 3,…

Osteogenesis Imperfect is also known as the, “Brittle Bone Disease”. This is an extremely rare disease with less than twenty thousand cases a year. As of today there is no known available cure, but there are treatments available to lessen the symptoms of the disease. This is a chronic illness that can last up to a few months, to lasting a person’s entire lifetime. This is a disease that causes extreme fragility in the bones of a normal person. This could make a person’s life extremely difficult…

1. Given the following amino acids, explain where they would be found in the tertiary structure of a protein and WHY (lack of explanation/incorrect explanations will NOT receive full credit; assume living system of pH = 7.4). Arg Phe Pro Glu His Ala Tyr Val Cys Arginine: This is a charged amino acid that is extremely hydrophilic. It is hydrophilic because while it has an aliphatic side chain that is hydrophobic, it also has two groups where a positive charge resonates between the two…

which contain cysteine, and cysteine has thiol. The more tightly coiled the hair filament is, the stronger the two-chain coil is. Keratin is made up of cells, intermerdiate filament, protofibril, protofilament, coil, and the helix. The cross sections is defined by the alpha keratins and richer amino acids: Ala, Val, Leu, Ile, Met, & Phe. The Disulfide link…

form is only present during the production of the protein, it will not be investigated in depth. Secondary structure in the 1WFB protein is peculiar – it contains no regular helices. Rather, it consists of one Coil which does not fit any specific helix classification. This coil encompasses the entire length of the protein except the final position…

PROTEIN STRUCTURE Proteins are polymers which is set up by 19 different α-amino acids and one imino acid (Proline) linked by amida bond or peptide bond. A protein usually contain amino acid residues, covalently linked, which spontaneously form a three-dimensional structure, based on the self-recognition of its respective sequence. Covalent bonds (peptide and disulfide), hydrogen bonds, electrostatic interactions, hydrophobic interactions, and weak, nonspecific attractive and repulsive forces are…