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A simple and novel interpretation of the three‐dimensional structure of globular proteins based on quantum‐mechanical computations on small model molecules. I
Author(s) -
Peters David,
Peters Jane
Publication year - 1985
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360240306
Subject(s) - rubredoxin , globular protein , chemistry , molecule , computation , ionic bonding , chemical physics , globular cluster , hydrogen bond , interpretation (philosophy) , ab initio , simple (philosophy) , computational chemistry , quantum , crystallography , molecular physics , physics , quantum mechanics , algorithm , computer science , ion , philosophy , organic chemistry , epistemology , galaxy , programming language
It is suggested that the three‐dimensional structure of globular proteins is partly determined by a framework of strengthened hydrogen bonds that involves both ionic side chains and water molecules in addition to the polypeptide backbone. This conclusion follows from a combination of the results of ab initio molecular‐orbital computations on small model molecules and high‐accuracy x‐ray data on the rubredoxin molecule. The computations yield the idea of hydrogen‐bonded bridges that are built from tens of atoms, and the experimental information yields the idea that the bridges are assembled into clusters, each of which is built from hundreds of atoms. Some 10 such clusters then form a globular protein.