✍ Scribed by Mikael Akke; Dr. Sture Forsén
No coin nor oath required. For personal study only.
To investigate the contribution to protein stability of electrostatic interactions between charged surface residues, we have studied the effect of substituting three negatively charged solvent exposed residues with their side‐chain amide analogs in bovine calbindin D~9k~—a small (M~r~ 8,500) globular protein of the calmodulin superfamily. The free energy of urea‐induced unfolding for the wildtype and seven mutant proteins has been measured. The mutant proteins have increased stability towards unfolding relative to the wildtype. The experimental results correlate reasonably well with theoretically calculated relative free energies of unfolding and show that electrostatic interactions between charges on the surface of a protein can have significant effects on protein stability.
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## Abstract The purpose of this investigation was to find new and more potent charge‐transfer probes for the study of certain aspects of polypeptide and protein conformation, especially of solvent‐exposure of aromatic amino‐acid side chains. N,N′‐dimethyl‐4,4′‐dipyridylium ion (paraquat) was shown
Previous ab initio computations revealed that the conformational building unit of the Ž . right-handed helix f y54Њ, f y45Њ is not an energy minimum on two-Ž Ä 4 . dimensional-type Ramachandran potential energy surfaces E s E , . Theoretical investigations were performed on several single-amino-acid