Hemoglobin and hair are both proteins, but they differ in structure due to their distinct functions and the types of amino acid sequences they contain. Hemoglobin is a globular protein, composed of four subunits that enable it to transport oxygen in the blood. In contrast, hair is primarily made of keratin, a fibrous protein that forms long, stable chains, providing strength and structure. These variations in amino acid composition and arrangement lead to their unique three-dimensional shapes and properties.
No, antibodies are not made of enzymes. Antibodies are Y-shaped proteins produced by the immune system and play a key role in identifying and neutralizing pathogens. Enzymes are a different type of protein that catalyze biochemical reactions in the body.
Analogous structures are structures that have the same function but different structures. They have evolved independently in different organisms to perform similar roles in response to similar environmental pressures. An example is the wings of birds and bats, which have different structures but both serve the same function of flight.
Myoglobin and hemoglobin both contain hydrophobic residues, but their distributions and roles differ due to their functions and structures. In myoglobin, hydrophobic residues are primarily located within the interior of the protein, stabilizing its compact structure and facilitating oxygen binding. In hemoglobin, hydrophobic residues also contribute to the stability of the protein, but they play a crucial role in the cooperative binding of oxygen through interactions between subunits. Thus, while both proteins have hydrophobic residues, their specific arrangements and functional implications vary according to their distinct roles in oxygen transport and storage.
Two specific examples of proteins that genes code for are hemoglobin and insulin. Hemoglobin, found in red blood cells, is responsible for transporting oxygen from the lungs to tissues throughout the body. Insulin, produced in the pancreas, regulates blood sugar levels by facilitating the uptake of glucose into cells. Both proteins play crucial roles in maintaining physiological functions in the body.
The amino acid sequences of hemoglobin in humans and frogs are different due to evolutionary divergence. While both hemoglobins are composed of similar building blocks (amino acids), the specific sequence of amino acids varies between species. This divergence in sequence reflects the adaptation of these proteins to meet the specific oxygen-carrying needs of each species.
practically no difference. In both the hemoglobin has the same job, bonding with oxygen.
ribosomes
different organism have dna with nucleotide base in a different order
Proteins and Carbohydrates are different because proteins are nutrients that help build and repair your cells. Proteins are any kind of meat and milk Ex. pork, liver, milk, and beans. Carbohydrates are sugars and starches. Ex. bread, milk, corn and other different things.
Proteins generally have both acidic (carboxyl) and basic (amino) functional groups in their structures. Depending on the pH of the surrounding environment, proteins can exist in different protonation states which can affect their overall charge and solubility. This contributes to the acid-base properties of proteins.
Hemoglobin is a protein and it has an iron ion that can attract an oxygen molecule to it. Both proteins and iron can be found in food.
No, antibodies are not made of enzymes. Antibodies are Y-shaped proteins produced by the immune system and play a key role in identifying and neutralizing pathogens. Enzymes are a different type of protein that catalyze biochemical reactions in the body.
Analogous structures are structures that have the same function but different structures. They have evolved independently in different organisms to perform similar roles in response to similar environmental pressures. An example is the wings of birds and bats, which have different structures but both serve the same function of flight.
Myoglobin and hemoglobin both contain hydrophobic residues, but their distributions and roles differ due to their functions and structures. In myoglobin, hydrophobic residues are primarily located within the interior of the protein, stabilizing its compact structure and facilitating oxygen binding. In hemoglobin, hydrophobic residues also contribute to the stability of the protein, but they play a crucial role in the cooperative binding of oxygen through interactions between subunits. Thus, while both proteins have hydrophobic residues, their specific arrangements and functional implications vary according to their distinct roles in oxygen transport and storage.
Two specific examples of proteins that genes code for are hemoglobin and insulin. Hemoglobin, found in red blood cells, is responsible for transporting oxygen from the lungs to tissues throughout the body. Insulin, produced in the pancreas, regulates blood sugar levels by facilitating the uptake of glucose into cells. Both proteins play crucial roles in maintaining physiological functions in the body.
The amino acid sequences of hemoglobin in humans and frogs are different due to evolutionary divergence. While both hemoglobins are composed of similar building blocks (amino acids), the specific sequence of amino acids varies between species. This divergence in sequence reflects the adaptation of these proteins to meet the specific oxygen-carrying needs of each species.
Hemoglobin is a protein carried by red blood cells to pick up oxygen in the lungs and deliver it to the peripheral tissues and maintain the viability of cells. it is made from two similar proteins that "stick together". these proteins must both be present for the hemoglobin to pick up and release oxygen. One of the proteins is called alpha, the other beta. Before birth, the beta protein is not expressed. A hemoglobin protein found only during fetal development, called gamma, substitutes up until birth. HemogLobin is the part of red blood cells that picks up oxygen in the lungs and releases it in your muscles, or wherever else it is needed.