why do serum protein molecules such as albumin and lysozyme adopt different changes within physiological pH range?
Proteins are molecules consisting of a linked chain of subunits called amino acids. Twenty different amino acids occur naturally. Different proteins (arising from different genes) will have different amino acid sequences. Each amino acid has a portion called a "side chain" that is unique in chemical composition and properties. The side chain can extend into the aqueous medium surrounding the protein. Some amino acids (glutamate, aspartate) have acidic side chains and so give up a H+ ion at physiological pH and leave the side chain with a "-" charge. Other amino acids (such as arginine and lysine) have basic side chains that tend to take up a H+ ion from the surrounding water and this confers a "+" charge on these units. Some amino acids (glycine, serine) do not interact with H+ ions at all. Thus, the net charge (sum of + and - charges) on any protein at a given pH is strictly a function of its amino acid composition. The pH that causes the net charge to be zero is called the isoelectric point and this parameter is measurable in the laboratory and can vary widely among different proteins.
before posting it try to google it because when i googled it the answe was right in front of me
you rlly don't have to write this who paragraph just take some that is important to your answer
The reason why serum protein molecules such as albumin and lysozyme adopt different changes within the physiological pH range lies in the fundamental principles of protein structure and electrostatic interactions.
Proteins are complex macromolecules composed of amino acids linked together by peptide bonds. Their structure is hierarchical, with primary, secondary, tertiary, and quaternary levels of organization.
At the primary level, proteins are linear chains of amino acids. Some amino acids contain charged side chains, which can either be positive (basic) or negative (acidic). The presence of these charged groups makes proteins amphoteric, meaning they can act as both acids and bases.
At physiological pH (approximately pH 7.4), the environment is slightly basic. The pH of a solution affects the protonation state of amino acid side chains within a protein molecule. Protonation refers to the addition or removal of a hydrogen ion (H+).
Albumin and lysozyme possess different amino acid compositions and arrangements, which influence their behavior at different pH values.
For example, albumin is predominantly negatively charged at physiological pH due to the abundance of acidic amino acid residues. This helps it maintain solubility and stability in the bloodstream. At lower pH values (more acidic conditions), the proportion of protonated (neutral) amino acid side chains increases, reducing the overall negative charge on the protein.
In contrast, lysozyme is positively charged at physiological pH due to the presence of basic amino acid residues. At higher pH values (more basic conditions), the protonation of acidic groups decreases, resulting in a decrease in the positive charge.
The changes in charge distribution within these protein molecules affect their interactions with other molecules, such as ligands and receptors, as well as their folding, stability, and function. These pH-induced changes in protein conformation are crucial for their proper functioning in the body.