ABSTRACT
Brownian computations were directed at Ribonuclease A (RNase A) and variants in folded states so as to quantify information of the statistical type at the atom/covalent bond level. This advanced the research reported in this journal last year on the information properties of enzyme primary structure. Brownian computation data are illustrated for a sixteen-member library. The results identify signature traits that distinguish the folded wild type (WT) molecule from variants. The distinctions are explainable in terms of correlated information and dispersion energy. The Brownian tools used for this study can be directed at other protein families (e.g., kinases, isomerases, etc.) in rapid screening, QSAR, and design applications.
Subject(s)
Protein Folding , Ribonuclease, Pancreatic/chemistry , Algorithms , Amino Acid Sequence , Models, Molecular , Protein Conformation , Protein Structure, Secondary , Protein Structure, Tertiary , Quantitative Structure-Activity Relationship , Ribonuclease, Pancreatic/metabolismABSTRACT
The information expressed in an enzyme's primary structure is investigated. Brownian computations are directed at Ribonuclease A (RNase A) so as to quantify the information at the atom/covalent bond level. The information content and distribution are crucial because the primary structure underpins the molecule's chemical functions. Brownian computation data are illustrated for the native protein, mutants, and sequence isomers. The results identify signature features of the active protein on new information grounds. The same tools offer rapid screening of proteins and polypeptides whereby several examples are illustrated.