title: Loop fold nature of globular proteins.
abstract: Protein chains make numerous returns in globules, thus forming loops, closed by tight residue-to-residue contacts-closed loops. Previous statistical analysis of the sizes and locations of the closed loops in all major protein folds revealed that the loops have an almost standard contour length of 25-30 amino acid residues and follow one after another along the chain. In this work the closed loops of the major folds are presented in three dimensions. A special image filtering procedure is introduced that allows one to visualize the standard size closed loops for the first time. The loop positions along the sequences are verified by detection of loop-end clusters.
authors.affiliation: Department of Structural Biology, The Weizmann Institute of Science, P.O.B. 26, Rehovot 76100, Israel. igor.berezovsky@weizmann.ac.il
authors.forename: I N
authors.initials: IN
authors.lastname: Berezovsky
authors.forename: E N
authors.initials: EN
authors.lastname: Trifonov
mesh_terms: D003627:Data Interpretation, Statistical; D019143:Evolution, Molecular; D021621:Imaging, Three-Dimensional; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins