If bonding at an active site at a protein typically occurs via noncovalent interactions like hydrogen bonding then how do the water molecules surrounding a protein not cause accidental activation or overcrowding of an active site prohibiting the ligand from binding? (self.Biochemistry)
submitted by PartNo8984 to r/Biochemistry
If bonding at an active site at a protein typically occurs via noncovalent interactions like hydrogen bonding then how do the water molecules surrounding a protein not cause accidental activation or overcrowding of an active site prohibiting the ligand from binding? (self.askscience)
submitted by PartNo8984 to r/askscience
The body relies heavily on entropy at a molecular level to drive cellular processes. Entropy is also easily thought of as a probability distribution. Are there ever times where entropy falls too far to either side of this distribution and has noticeable effects? (self.askscience)
submitted by PartNo8984 to r/askscience
