S. Rackovsky
Cornell University
46 Papers
665 Citations
S. Rackovsky is an academic researcher from Cornell University. The author has contributed to research in topics: Protein structure & Protein structure prediction. The author has an hindex of 19, co-authored 46 publications. Previous affiliations of S. Rackovsky include University of Rochester & Icahn School of Medicine at Mount Sinai.
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Papers
Prediction of protein conformation on the basis of a search for compact structures: Test on avian pancreatic polypeptide
TL;DR: Application of this procedure to the 36‐residue avian pancreatic polypeptide led to a structure that resembled the one determined by X‐ray crystallography; it had an α‐helix starting at residue 13, with the N‐terminal portion of the chain in an extended conformation packed against the α‐ Helix.
“Hidden” sequence periodicities and protein architecture
TL;DR: It is shown that, although the frequencies of the signals characteristic of a particular architecture have definite wave numbers, they can occur in any physical property.
70
Lessons from application of the UNRES force field to predictions of structures of CASP10 targets
Yi He,Magdalena A. Mozolewska,Magdalena A. Mozolewska,Paweł Krupa,Paweł Krupa,Adam K. Sieradzan,Tomasz K Wirecki,Tomasz K Wirecki,Adam Liwo,Khatuna Kachlishvili,S. Rackovsky,S. Rackovsky,Dawid Jagieła,Rafał Ślusarz,Cezary Czaplewski,Stanisław Ołdziej,Harold A. Scheraga +16 more
TL;DR: It is shown that the physics-based approach for protein-structure prediction can lead to exceptionally good results when correct domain packing is an issue, even for a highly homologous target, and that it has the ability to predict domain–domain orientations, which is a significant advance in the state of the art.
70
Correlation of the structure of the transmembrane domain of the neu oncogene-encoded p185 protein with its function.
TL;DR: If the intracellular concentration of the normal protein is increased at least 10-fold, thereby increasing the alpha-helical form by this factor, cell transformation should result, according to conformational energy analysis based on ECEPP.
56
On the properties and sequence context of structurally ambivalent fragments in proteins.
Igor B. Kuznetsov,S. Rackovsky +1 more
TL;DR: It is shown that each type of SAP has an unusual, type‐specific amino acid composition and, as a result, simultaneous intrinsic preferences for two distinct types of backbone conformation, which has implications for protein design and structure prediction.