Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Markandeswar Panda"'
Autor:
Markandeswar Panda, Judith A. Walmsley
Publikováno v:
The Journal of Physical Chemistry B. 115:6377-6383
Concentration and temperature dependent studies of the circular dichroism of dianionic guanosine 5'-monophosphate (5'-GMP), where the cation was Na(+), K(+), or Rb(+) ion, were done to obtain information regarding the nature of the self-assembled 5'-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e914d4b7be8c5f36128d739e435dbe2
https://doi.org/10.1021/jp201630g
https://doi.org/10.1021/jp201630g
Autor:
Markandeswar Panda, Subas C. Pati
Publikováno v:
Bulletin des Sociétés Chimiques Belges. 91:271-281
Kinetics of ruthenium (III) chloride catalysed oxidation of acetone, ethyl methyl ketone, isobutylmethyl ketone, pentan-2-one, cyclopentanone and cyclohexanone by sodium metaperiodate in aqueous alkaline medium at constant ionic strength is reported.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cfd58625abf4becc5dda19219eff5113
https://doi.org/10.1002/bscb.19820910403
https://doi.org/10.1002/bscb.19820910403
Publikováno v:
Protein Science. 9:536-543
A dominant feature of folding of cytochrome c is the presence of nonnative His-heme kinetic traps, which either pre-exist in the unfolded protein or are formed soon after initiation of folding. The kinetically trapped species can constitute the major
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::055d1083d1ce232ebdb0940934f5fd85
https://doi.org/10.1110/ps.9.3.536
https://doi.org/10.1110/ps.9.3.536
Publikováno v:
Biochemistry. 45:746-754
Subunits located near the cardiolipin binding sites of bovine heart cytochrome c oxidase (CcO) were identified by photolabeling with arylazido-cardiolipin analogues and detecting labeled subunits by reversed-phase HPLC and HPLC–electrospray ionizat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::816aea557b369163ea6a04f9456a6939
https://doi.org/10.1021/bi050870z
https://doi.org/10.1021/bi050870z
Autor:
Satya Prakash Panda, Yuzuru Ishimura, Bettie Sue Siler Masters, Markandeswar Panda, Jung-Ja P. Kim, M. Jáchymová, Linda J. Roman, Thomas M. Shea, Pavel Martásek
Publikováno v:
Proceedings of the National Academy of Sciences. 102:15833-15838
At least three building blocks are responsible for the molecular basis of the modulation of electron transfer in nitric oxide synthase (NOS) isoforms: the calmodulin-binding sequence, the C-terminal extension, and the autoregulatory loop in the reduc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8209822c2274e0cf8197227def5de0ca
https://doi.org/10.1073/pnas.0506522102
https://doi.org/10.1073/pnas.0506522102
Publikováno v:
Biochemistry. 41:12843-12849
We investigated the dissociation of single-ring heptameric GroEL (SR1) by high hydrostatic pressure in the range of 1-2.5 kbar. The kinetics of the dissociation of SR1 in the absence and presence of Mg2+, KCl, and nucleotides were monitored using lig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97c99007fa5025348bbe1851cbd0c877
https://doi.org/10.1021/bi020366j
https://doi.org/10.1021/bi020366j
Autor:
Paul M. Horowitz, Markandeswar Panda
Publikováno v:
Biochemistry. 41:1869-1876
We investigated the dissociation of tetradecameric GroEL by high hydrostatic pressure in the range of 1-2.5 kbar. Kinetics of the dissociation of GroEL in the absence and presence of Mg(2+) and/or KCl were monitored using light scattering. All of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd59c5781efcbe11b8931251b8011ed3
https://doi.org/10.1021/bi011794c
https://doi.org/10.1021/bi011794c
Autor:
and Alan R. Fersht, Alison L. Smoot, Markandeswar Panda, Bill T. Brazil, Ashley M. Buckle, Paul M. Horowitz
Publikováno v:
Biochemistry. 40:4484-4492
The extent of hydrophobic exposure upon bis-ANS binding to the functional apical domain fragment of GroEL, or minichaperone (residues 191-345), was investigated and compared with that of the GroEL tetradecamer. Although a total of seven molecules of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7838cc4955d6256b9e6793e68f174b79
https://doi.org/10.1021/bi001822b
https://doi.org/10.1021/bi001822b
Publikováno v:
Journal of Biological Chemistry. 275:63-70
The competition between protein aggregation and folding has been investigated using rhodanese (thiosulfate:cyanide sulfurtransferase, EC 2.8.1.1) as a model. During folding from a urea-denatured state, rhodanese rapidly forms associated species or in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b02f90e4c918a25232f9a6c32869a2dc
https://doi.org/10.1074/jbc.275.1.63
https://doi.org/10.1074/jbc.275.1.63
Autor:
Subas C. Pati, Markandeswar Panda
Publikováno v:
International Journal of Chemical Kinetics. 28:453-460
The kinetics of Ruthenium(III) chloride mediated oxidation of acetone, 2-butanone, 4-methyl-2-pentanone, 2-pentanone, cyclopentanone, and cyclohexanone by sodium periodate in aqueous HClO4 media was zero-order in [IO4−] and first-order in [ketone].
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::77152f6213134ad2fc788aae629704c8
https://doi.org/10.1002/(sici)1097-4601(1996)28:6<453::aid-kin7>3.0.co
https://doi.org/10.1002/(sici)1097-4601(1996)28:6<453::aid-kin7>3.0.co