title: Backbones of folded proteins reveal novel invariant amino acid neighborhoods.
abstract: Folding of naturally occurring proteins has eluded a universal molecular level explanation till date. Rather, there is an abundance of diverse views on dominant factors governing protein folding. Through rigorous analyses of several thousand crystal structures, we observe that backbones of folded proteins display some remarkable invariant features. Folded proteins are characterized by spatially well-defined, distance dependent, and universal, neighborhoods of amino acids which defy any of the conventionally prevalent views. These findings present a compelling case for a newer view of protein folding which takes into account solvent mediated and amino acid shape and size assisted optimization of the tertiary structure of the polypeptide chain to make a functional protein.
authors.affiliation: School of Biological Sciences, Indian Institute of Technology Delhi, New Delhi, India. amittal@bioschool.iitd.ac.in
authors.forename: Aditya
authors.initials: A
authors.lastname: Mittal
authors.forename: B
authors.initials: B
authors.lastname: Jayaram
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000235:genetics
chemical_list: D000596:Amino Acids; D011506:Proteins