Zobrazeno 1 - 7
of 7
pro vyhledávání: '"V. V. Hemanth Giri Rao"'
Autor:
V V Hemanth Giri Rao, Shachi Gosavi
Publikováno v:
PLoS Computational Biology, Vol 10, Iss 11, p e1003938 (2014)
Having multiple domains in proteins can lead to partial folding and increased aggregation. Folding cooperativity, the all or nothing folding of a protein, can reduce this aggregation propensity. In agreement with bulk experiments, a coarse-grained st
Externí odkaz:
https://doaj.org/article/a089eb39dc5f4233957b5b24db70e728
Autor:
V. V. Hemanth Giri Rao, Shachi Gosavi
Publikováno v:
Proceedings of the National Academy of Sciences. 115:1998-2003
For successful protease inhibition, the reactive center loop (RCL) of the two-domain serine protease inhibitor, α1-antitrypsin (α1-AT), needs to remain exposed in a metastable active conformation. The α1-AT RCL is sequestered in a β-sheet in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::274fc98e3c68f59ec789e2eb1b976d64
https://doi.org/10.1073/pnas.1708173115
https://doi.org/10.1073/pnas.1708173115
Publikováno v:
The Journal of Physical Chemistry B. 120:12064-12078
Escherichia coli cytolysin A (ClyA) is an α-helical pore-forming toxin (PFT) which lyses target cells by forming membrane permeabilizing pores. The rate-determining step of this process is the conversion of the soluble ClyA monomer into a membrane i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d18d5fdc1c2f54d7a00635c6039d6e5
https://doi.org/10.1021/acs.jpcb.6b09400
https://doi.org/10.1021/acs.jpcb.6b09400
Autor:
Shachi Gosavi, V. V. Hemanth Giri Rao
Publikováno v:
Current Opinion in Structural Biology. 36:67-74
Proteins fold on a biologically-relevant timescale because of a funnel-shaped energy landscape. This landscape is sculpted through evolution by selecting amino-acid sequences that stabilize native interactions while suppressing stable non-native inte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66ba97ca63760565a48fe90baa907743
https://doi.org/10.1016/j.sbi.2016.01.001
https://doi.org/10.1016/j.sbi.2016.01.001
Autor:
V. V. Hemanth Giri Rao, Shachi Gosavi
Publikováno v:
The Journal of Physical Chemistry B. 119:11203-11214
The interleukin-1 cytokines belong to the β-trefoil fold family and play a key role in immune responses to infections and injury. We simulate the structure-based models of two interleukin-1 cytokines, IL-33 and IL-1β, and find that IL-33 has a lowe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b75d637a1b011a74f9f872277bd81dd5
https://doi.org/10.1021/acs.jpcb.5b03111
https://doi.org/10.1021/acs.jpcb.5b03111
Publikováno v:
Israel Journal of Chemistry. 54:1230-1240
Natural proteins have evolved amino acid sequences that provide a native-structural bias to folding. Structure-based models (SBMs) of proteins ignore all non-native interactions and encode this bias by including only interactions present in the nativ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b29e0bd978ceaae81378bd1ff634086c
https://doi.org/10.1002/ijch.201400035
https://doi.org/10.1002/ijch.201400035
Publikováno v:
Biophysical Journal. 116:471a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7cb1c9b23bbe919bd6f0a48e4aba0d58
https://doi.org/10.1016/j.bpj.2018.11.2546
https://doi.org/10.1016/j.bpj.2018.11.2546