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pro vyhledávání: '"K. Tejaswi Naidu"'
Polyols, increasing global stability of cytochrome c, destabilize the thermal unfolding intermediate
Autor:
K. Tejaswi Naidu, N. Prakash Prabhu
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 40:11216-11228
Studies on the intermediate states of proteins provide essential information on folding pathway and energy landscape of proteins. Osmolytes, known to alter the stability of proteins, might also aff...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7835207117c100309a461737fa0a18fb
https://doi.org/10.1080/07391102.2021.1956593
https://doi.org/10.1080/07391102.2021.1956593
Autor:
Rituparna Chakrabarti, Sushmitha Duddu, Ashutosh Tiwari, K. Tejaswi Naidu, Pooja Sharma, Nishant Chakravorty, Praphulla Chandra Shukla
Publikováno v:
Life Sciences. 321:121620
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5fc240482b637638241891df568c6a1f
https://doi.org/10.1016/j.lfs.2023.121620
https://doi.org/10.1016/j.lfs.2023.121620
Publikováno v:
The Journal of Physical Chemistry B. 124:10077-10088
Osmolytes are known to stabilize proteins under stress conditions. Thermal denaturation studies on globular proteins (β-lactoglobulin, cytochrome c, myoglobin, α-chymotrypsin) in the presence of ethylene glycol (EG), a polyol class of osmolyte, dem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a873c235ddc391a58635b7cb76b67f9
https://doi.org/10.1021/acs.jpcb.0c06247
https://doi.org/10.1021/acs.jpcb.0c06247
Autor:
K. Tejaswi Naidu, N. Prakash Prabhu
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 40:820-832
Osmolytes are known to stabilize proteins against denaturing conditions. Ethylene glycol (EG), however, shows a distinctive effect on α-lactalbumin (α-LA) that it stabilizes the protein against cold-induced denaturation, whereas it destabilizes dur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65ea7bd770d1f696dc569348ce32c608
https://doi.org/10.1080/07391102.2020.1819422
https://doi.org/10.1080/07391102.2020.1819422
Autor:
K. Tejaswi Naidu, N. Prakash Prabhu
Publikováno v:
The journal of physical chemistry. B. 115(49)
Protein-surfactant interaction is widely studied to understand stability and structural changes in proteins. In this Article, we have investigated SDS-induced unfolding of RNase A using absorbance, intrinsic fluorescence of the protein, anisotropy, T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b0c44f16a8aa07fb5736d656f09a87d
https://pubmed.ncbi.nlm.nih.gov/22014160
https://pubmed.ncbi.nlm.nih.gov/22014160
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