globular proteins

I don't understand how globular proteins are soluble in water.

I understand it has a hydrophilic r groups on the outside so these would be soluble due to polar water molecules surrounding the r groups but what about the hydrophobic internal structure. this is not polar so won't dissolve and is part of the globular protein so how does the globular protein dissolve if the hydrophobic r groups don't interact with water

does it leave the hydrophobic r groups without any protection from the hydrophilic r groups due to them being dissolved

so how does that make it soluble in blood if you don't mind me asking if the hydrophobic doesn't dissolve

thanks for your help. I was getting confused with my knowledge on solubility. so it's not like NACL when the ions are seperated by polar water molecules but rather the water surrounding the external surface of the protein(ie hydrophilic)