Why do globular proteins fit the limited set of folding patterns?
By A. V. Finkelstein, O. Ptitsyn. 1987
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
- Kuo-Chen Chou
- Hua Cheng
- Nick V. Grishin
- Bong-Hyun Kim
- Hongbin Shen
- Hong-Bin Shen
- Steven E. Brenner
- Cyrus Chothia
Citations in the corpus
- REVIEW : Recent advances in developing web-servers for predicting protein attributes (2009, background): “Its underpinning is based on the assumption that the number of protein folds is limited [228-231].”
- Ensemble classifier for protein fold pattern recognition (2006, methodology): “In this paper, we shall resort to the taxonomic approach, whose underpinning is based on the assump-* tion that the number of protein folds is limited (Chou & Zhang, 1995; Dubchak et al., 1999; Finkelstein & Ptitsyn, 1987; Murzin et al., 1995).”
- HorA web server to infer homology between proteins using sequence and structural similarity (2009, background): “Such ‘analogous’ similarity often comes from convergence to similar structures due to a limited number of energetically favorable ways to pack secondary structural elements (SSEs) ( 8 ,9).”
- Discrimination between distant homologs and structural analogs: lessons from manually constructed, reliable data sets. (2008, methodology): “A.3. Intramolecule structure scores ( 1 ) DALI score (dali)”
- SCOP: a structural classification of proteins database for the investigation of sequences and structures. (1995, background): “These regularities arise from the intrinsic physical and chemical properties of proteins (Chothia, 1984; Finkelstein & Ptitsyn, 1987) and provide the basis for the classification of protein folds (Levitt & Chothia, 1976; Richardson, 1981).”