Turkey hemoglobin would likely have the least differences with chicken hemoglobin, as both species are avians and share a more recent common ancestor compared to mammals like humans, gorillas, horses, and kangaroos. The evolutionary closeness of chickens and turkeys suggests that their hemoglobin sequences would be more similar due to fewer genetic divergences. In contrast, the other mammals would have accumulated more differences over time, leading to greater variation in their hemoglobin sequences.
Each organism's individuality haemoglobin is different in the sense that it varies based on composition, and each organism has a separate cell life based composition, affecting the haemoglobin.
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.
The DNA code for normal hemoglobin is the gene that encodes for the production of the protein hemoglobin. The sequence of this gene includes instructions for building the alpha and beta globin chains that make up the hemoglobin protein. This gene is located on chromosome 11 in humans.
Yes, sickle-cell disease is caused by a genetic mutation in the hemoglobin gene, resulting in an error in the amino acid sequence of the hemoglobin protein. This mistake leads to the production of abnormal hemoglobin that causes red blood cells to become sickle-shaped, leading to various health problems.
Hemoglobin is used for molecular phylogenetic analysis to study evolutionary relationships between organisms because its structure and sequence can reveal similarities and differences among different species. By comparing the sequences of hemoglobin protein across different organisms, researchers can construct phylogenetic trees to determine the evolutionary relationships and common ancestors between species. This information is crucial for understanding evolutionary history and the relatedness between different organisms.
There are no differences in the amino acids in human hemoglobin and wolf hemoglobin.
Each organism's individuality haemoglobin is different in the sense that it varies based on composition, and each organism has a separate cell life based composition, affecting the haemoglobin.
There are no differences in the amino acids in human hemoglobin and wolf hemoglobin.
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.
These are called the second differences. If they are all the same (non-zero) then the original sequence is a quadratic.
A quadratic sequence is a sequence of numbers in which the difference between consecutive terms changes at a constant rate. To identify the rule, first calculate the first differences (the differences between consecutive terms) and then the second differences (the differences of the first differences). If the second differences are constant, the sequence is quadratic. The general form of a quadratic sequence can be expressed as ( an^2 + bn + c ), where ( n ) is the term number, and ( a ), ( b ), and ( c ) are constants.
Nucleotide sequence, human, hemoglobin
The DNA code for normal hemoglobin is the gene that encodes for the production of the protein hemoglobin. The sequence of this gene includes instructions for building the alpha and beta globin chains that make up the hemoglobin protein. This gene is located on chromosome 11 in humans.
Yes, sickle-cell disease is caused by a genetic mutation in the hemoglobin gene, resulting in an error in the amino acid sequence of the hemoglobin protein. This mistake leads to the production of abnormal hemoglobin that causes red blood cells to become sickle-shaped, leading to various health problems.
Hemoglobin is used for molecular phylogenetic analysis to study evolutionary relationships between organisms because its structure and sequence can reveal similarities and differences among different species. By comparing the sequences of hemoglobin protein across different organisms, researchers can construct phylogenetic trees to determine the evolutionary relationships and common ancestors between species. This information is crucial for understanding evolutionary history and the relatedness between different organisms.
4,8,12,16,20
0,1,1,2,3,5,8,13