Article
Thermodynamic effects of proline introduction on protein stability.
Proteins - 1 Feb 2007
Prajapati Ravindra Singh, Das Mili, Sreeramulu Sridhar, Sirajuddin Minhajuddin, Srinivasan Sankaranarayanan, Krishnamurthy Vaishnavi, Ranjani Ranganathan, Ramakrishnan C, Varadarajan Raghavan
Abstract excerpt
The amino acid Pro is more rigid than other naturally occurring amino acids and, in proteins, lacks an amide hydrogen. To understand the structural and thermodynamic effects of Pro substitutions, it was introduced at 13 different positions in four different proteins, leucine-isoleucine-valine binding protein, maltose binding protein, ribose binding protein, and thioredoxin. Three of the maltose binding protein...
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