It is a protein that is stretchable during dissolutions.
Albumin and globulin are simple soluble proteins.
An elastic soluble protein is a protein that can stretch or deform and dissolve in water. These proteins typically have high elasticity and solubility properties, making them useful in various biological functions such as muscle contraction or cell structure. Examples include elastin, collagen, and keratin.
protein will have a net positive charge due to the protonation of all basic side chains (NH3+) in its structure therefore it will be soluble. If there is a charge at the protein surface, the protein prefers to interact with water, rather than with other protein molecules so makes it more soluble.
The RNA molecules that attach the amino acid to the protein chain are usually soluble.
hi
No, epinephrine is not lipid soluble. It is a water-soluble hormone that acts on G-protein-coupled receptors on the cell surface to exert its physiological effects.
No it is not soluble in water it is soluble in chloroform, alcohol, methnol
Protein is generally not soluble in acetone. Acetone is a polar solvent and proteins are typically complex molecules with hydrophilic and hydrophobic regions that interact more favorably with water. Proteins are usually soluble in water or buffers that mimic cellular environments.
Growth hormone is water soluble. It is a protein hormone that circulates in the blood and interacts with cell surface receptors to exert its effects on growth and metabolism.
chloride salts are usually soluble, but with silver it is not soluble.
No, soap is not soluble in oil. Soap is hydrophilic, meaning it is soluble in water, but not in oils or other nonpolar substances.
You can't. But consider... 1. ...that very few proteins are insoluble in their native context (that of a living organism), meaning that your attempts to mimic the conditions that the protein normally sees have failed so far. So you can try alternative conditions to make it soluble (different salts, etc). 2. ...that many proteins are composed of independently-folded modules ('domains'), and individual modules can be made and purified in isolation of the others. These isolated domains might be soluble even if the whole protein is not.