Entropy calculations on the molten globule state of a protein: side-chain entropies of alpha-lactalbumin.
- We present entropy estimates based on molecular dynamics simulations of models of the molten globule state of the protein alpha-lactalbumin at low pH. The entropy calculations use the covariance matrix of atom-positional fluctuations and yield the complete configurational entropy. The configurational entropy of the entire protein and of each of its side chains is calculated. Exposed side chains show a larger entropy compared to buried side chains. A comparison to data from rotamer counting is made and significant differences are found.
- Publication status:
- Publisher copy:
- Copyright date:
If you are the owner of this record, you can report an update to it here: Report update to this record