R
Ramanathan Sowdhamini
Researcher at National Centre for Biological Sciences
Publications - 290
Citations - 5057
Ramanathan Sowdhamini is an academic researcher from National Centre for Biological Sciences. The author has contributed to research in topics: Biology & Protein domain. The author has an hindex of 33, co-authored 256 publications receiving 4458 citations. Previous affiliations of Ramanathan Sowdhamini include Birkbeck, University of London & Tata Institute of Fundamental Research.
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Journal ArticleDOI
Knowledge-Based Protein Modeling
TL;DR: While many models are still constructed at least in part by manual methods on graphics devices, automated procedures have come into greater use and include those that assemble fragments of structure from other known structures and those that derive coordinates for the model from the satisfaction of restraints placed on atomic positions.
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Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis
Ramanathan Sowdhamini,Narayanaswamy Srinivasan,Brian K. Shoichet,Daniel V. Santi,C. Ramakrishnan,Padmanabhan Balaram +5 more
TL;DR: A computer modeling procedure for assessing the stereochemical suitability of pairs of residues in proteins as potential sites for introduction of cystine disulfide crosslinks has been developed and two positions for the introduction of 'stereochemically optimal' disulfides are identified in subtilisin.
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Molecular evolution and domain structure of plasminogen-related growth factors (HGF/SF and HGF1/MSP).
Luis Enrique Donate,Narayanaswamy Srinivasan,Ramanathan Sowdhamini,Ermanno Gherardi,Tom L. Blundell,Samuel Aparicio +5 more
TL;DR: Models of the N domains of HGF/SF, HGF1/MSP, and plasminogen, characterized by the presence of 4 conserved Cys residues forming a loop in a loop, have been modeled based on disulfide‐bond constraints and suggest a mechanism for the formation of a noncovalent H GF/SF homodimer that may be responsible for the activation of the Met receptor.
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Conformations of disulfide bridges in proteins
TL;DR: Disulfide bridging across antiparallel extended strands is observed in alpha-lytic protease, crambin, and beta-trypsin and this structure is shown to be very similar to those obtained in small cystine peptides.
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Nanoscale organization of hedgehog is essential for long-range signaling
Neha Vyas,Debanjan Goswami,A. Manonmani,Pranav Sharma,Hassan Annegowda Ranganath,K. VijayRaghavan,L. S. Shashidhara,Ramanathan Sowdhamini,Satyajit Mayor +8 more
TL;DR: It is found that cell-surface Hh forms suboptical oligomers, further concentrated in visible clusters colocalized with HSPGs, and exhibits a hierarchical organization from the nanoscale to visible clusters with distinct functions.