Globular proteins

• Globular proteins are a specific category of proteins with various functions.
• The overall 3D structure of a protein is determined by the primary structure and the 3D shape determines the type of protein.
• Globular proteins can either be fibrous or globular.
• Globular proteins are spherical in shape, have hydrophobic residues on the inside and hydrophilic residues on the outside, and are soluble in water.
• Globular proteins have specific shapes or 3D shapes that allow them to carry out specific functions.
• Enzymes are an example of globular proteins with specific shapes or 3D shapes that allow them to carry out particular reactions.
• Hemoglobin is an example of a globular protein with a specific shape that allows it to transport oxygen from the lungs to the body tissues.
• Insulin is an example of a globular protein that is hormone that flows through the blood dissolved in the blood plasma.
• Insulin is a globular protein and a hormone made and secreted by the pancreas, which helps maintain blood glucose concentration in the blood.
• Insulin is composed of two polypeptide chains, one with an alpha helix on its end and the other with a beta-pleated sheet.
• The two polypeptide chains in insulin are joined together by dis.
• The polypeptide chain with an alpha helix on its end is called the a chain, and the other is called the b chain.
• Hemoglobin can transport four oxygen molecules due to the four polypeptides and four prosthetic groups it contains.
• Each polypeptide chain in hemoglobin has its own prosthetic group, known as a heme group, which contains an iron ion with a two plus charge.
• Hemoglobin is a protein made up of four polypeptide chains, each with a quarternary structure.
• Hemoglobin is described as a conjugated protein due to the prosthetic group attached to each polypeptide chain.
• Pepsin is an example of a globular protein that is an enzyme dissolved in the cells or the outer cells environment.
• The shape of insulin makes it globular and allows it to specifically bind to insulin receptors on the membranes of certain cells, helping to lower blood glucose concentration.
• Insulin as a hormone has hydrophilic r groups on its outside, making it soluble in water and allowing it to travel in the water, transport around the body, and dissolve in the blood.
• Globular proteins can also be enzymes such as pepsin, which catalyzes digestion of proteins.
• Pepsin, an example of a globular protein, exists in the stomach, which has a very acidic environment with a low pH of around 2.
• Most proteins would be denatured at such a low pH because they contain some amino acids with basic r groups, but pepsin has a primary structure with very few basic r groups, so its tertiary structure is not affected by the low pH.
• Ulfide links or disulfide bridges are formed by amino acids containing sulfur atoms.
• The tertiary structure of pepsin is kept stable and in the same shape by the hydrogen bonds and the disulfide links between various amino acids.