Jump to content

Recommended Posts

Posted

Probably Molecular Biology 101, but I was wondering if anyone could tell me how an amino acid's pKa can be altered by protein environments and also by surrounding charge?

 

e.g. Glutatate and aspartate can hold onto protons around the physiological pH in some instances (microenvironment and surrounding charge) when their pKa is much lower - how do they do this!

  • 2 months later...
Posted
Probably Molecular Biology 101, but I was wondering if anyone could tell me how an amino acid's pKa can be altered by protein environments and also by surrounding charge?

 

e.g. Glutatate and aspartate can hold onto protons around the physiological pH in some instances (microenvironment and surrounding charge) when their pKa is much lower - how do they do this!

 

It has to do with the situation. If hydrogen bonding networks established are unable to be interrupted then the proton will remain attached to the amino acid.

 

Protein shape can also have an effect. If the shape is such that it shields the side chains from outside effects, then the proton will be unable to leave.

Create an account or sign in to comment

You need to be a member in order to leave a comment

Create an account

Sign up for a new account in our community. It's easy!

Register a new account

Sign in

Already have an account? Sign in here.

Sign In Now
×
×
  • Create New...

Important Information

We have placed cookies on your device to help make this website better. You can adjust your cookie settings, otherwise we'll assume you're okay to continue.