Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Vasam Manjveekar Prabantu"'
Autor:
Vasundhara Gadiyaram, Vasam Manjveekar Prabantu, Arinnia Anto Manjaly, Ananth Muthiah, Saraswathi Vishveshwara
Publikováno v:
Current Research in Structural Biology, Vol 7, Iss , Pp 100147- (2024)
The function of a protein is most of the time achieved due to minute conformational changes in its structure due to ligand binding or environmental changes or other interactions. Hence the analysis of structure of proteins should go beyond the analys
Externí odkaz:
https://doaj.org/article/543e27fd4a7b4f9d939908b3670a2073
Autor:
Nagarajan Naveenkumar, Vasam Manjveekar Prabantu, Sneha Vishwanath, Ramanathan Sowdhamini, Narayanaswamy Srinivasan
Publikováno v:
FEBS Open Bio, Vol 12, Iss 12, Pp 2147-2153 (2022)
Homologous proteins can display high structural variation due to evolutionary divergence at low sequence identity. This classical inverse relationship between sequence identity and structural similarity, established many years ago, has remained true
Externí odkaz:
https://doaj.org/article/bd5995f442e94089a7ac171b8e31a102
Autor:
Vasam Manjveekar Prabantu, Vasundhara Gadiyaram, Saraswathi Vishveshwara, Narayanaswamy Srinivasan
Publikováno v:
Current Research in Structural Biology, Vol 4, Iss , Pp 134-145 (2022)
Proteins perform their function by accessing a suitable conformer from the ensemble of available conformations. The conformational diversity of a chosen protein structure can be obtained by experimental methods under different conditions. A key issue
Externí odkaz:
https://doaj.org/article/74aea45c16ad4eaba06795c4df258f35
Publikováno v:
Frontiers in Molecular Biosciences, Vol 7 (2021)
The interactions between residues in a protein tertiary structure can be studied effectively using the approach of protein structure network (PSN). A PSN is a node-edge representation of the structure with nodes representing residues and interactions
Externí odkaz:
https://doaj.org/article/272bce9c1edc4763bfaa000d581bbd6b
Autor:
Vasam Manjveekar Prabantu, Vasundhara Gadiyaram, Saraswathi Vishveshwara, Narayanaswamy Srinivasan
Publikováno v:
Current research in structural biology. 4
Proteins perform their function by accessing a suitable conformer from the ensemble of available conformations. The conformational diversity of a chosen protein structure can be obtained by experimental methods under different conditions. A key issue
Publikováno v:
Frontiers in Molecular Biosciences, Vol 7 (2021)
Frontiers in Molecular Biosciences
Frontiers in Molecular Biosciences
The interactions between residues in a protein tertiary structure can be studied effectively using the approach of protein structure network (PSN). A PSN is a node-edge representation of the structure with nodes representing residues and interactions
Autor:
Andrew J. Armstrong, Claudia Bank, Ramray Bhat, Erez Braun, Eric Brenner, Amy Brock, Jean-Pascal Capp, Marco Casali, Lynn Chiu, Narendra M. Dixit, Pedro M. Enriquez-Navas, Robert A. Gatenby, Scott F. Gilbert, Philip Greulich, Dongya Jia, Kaitlyn Johnson, Mohit Kumar Jolly, Anastasiya V. Kharlamova, Sandeep Krishna, Prakash Kulkarni, Saurav Kumar, Caterina A.M. La Porta, Jimpi Langthasa, Sunil Laxman, Herbert Levine, Nicholas A. Levis, Ben D. MacArthur, Kenneth Z. McKenna, Francesca Merlin, Vidyanand Nanjundiah, Anusha Nathan, Stuart A. Newman, H. Frederik Nijhout, José N. Onuchic, Pranesh Padmanabhan, András Páldi, David W. Pfennig, Vasam Manjveekar Prabantu, Rubesh Raja, Annapoorni Rangarajan, Govindan Rangarajan, Erzsébet Ravasz Regan, Sarthak Sahoo, Ravi Salgia, Purba Sarkar, Maya U. Sheth, Rosanna Smith, Jill A. Soha, Jason A. Somarelli, Narayanaswamy Srinivasan, Dragan Stajic, Ayalur Raghu Subbalakshmi, Ananthalakshmy Sundararaman, Yuichiro Suzuki, Lyudmila N. Trut, Mick F. Tuite, Günter Vogt, Jin Wang, Kathryn E. Ware, Li Xu, Arangasamy Yazhini, Stefano Zapperi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::07a0fef28deacf97a05914ed947a59c9
https://doi.org/10.1016/b978-0-12-817996-3.00032-3
https://doi.org/10.1016/b978-0-12-817996-3.00032-3
The discovery of moonlighting proteins has opened the paradigm of one protein with many functions. Proteins can switch their functions or functional levels through cellular environmental cues and structural changes without altering their amino acid s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5c27dfc1ce72bc71db1c3dc37a8db073
https://doi.org/10.1016/b978-0-12-817996-3.00006-2
https://doi.org/10.1016/b978-0-12-817996-3.00006-2