Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Francesca Catanzano"'
Autor:
Giuseppe Graziano, Francesca Catanzano
Publikováno v:
Journal of Thermal Analysis and Calorimetry. 91:61-66
Bovine seminal ribonuclease is the only pancreatic-type ribonuclease to possess a dimeric structure: the two identical subunits are covalently linked by two disulfide bridges. Actually, the protein exists in two different dimeric structures owing to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0f6f2954f012fe45df6803bcf46578fe
https://doi.org/10.1007/s10973-007-8537-2
https://doi.org/10.1007/s10973-007-8537-2
Autor:
Giuseppe Graziano, Francesca Catanzano
Publikováno v:
Journal of Thermal Analysis and Calorimetry. 91:57-60
It is well established that the reversible thermal denaturation of small globular proteins is a cooperative two-state transition, analogous to a first-order phase transition in a finite-size system. Finite-size effects on the cooperativity of the rev
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::10d93c402569bd80a9df83a7e1399c44
https://doi.org/10.1007/s10973-007-8536-3
https://doi.org/10.1007/s10973-007-8536-3
Publikováno v:
Thermochimica Acta. 364:165-172
In this study a careful analysis of the enthalpic and entropic effects associated with the removal of each of the four disulfide bridges in ribonuclease A is accomplished. The fundamental role of disulfides for the stability of the native structure i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7385047e1a08fb4d923b1fc8205ba327
https://doi.org/10.1016/s0040-6031(00)00646-8
https://doi.org/10.1016/s0040-6031(00)00646-8
Publikováno v:
Thermochimica Acta. 345:59-66
In this study the pH dependence of the thermodynamic stability of tendamistat is analyzed. This small globular protein of 74 residues shows a very marked dependence of thermal stability on pH: the denaturation temperature increases from 68.9°C at pH
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6fe3e0e440a2686bd6f01bf46adb31f7
https://doi.org/10.1016/s0040-6031(99)00350-0
https://doi.org/10.1016/s0040-6031(99)00350-0
Publikováno v:
Journal of Biological Chemistry. 275:895-900
A NAD(P)H oxidase has been isolated from the archaeon Sulfolobus solfataricus. The enzyme is a homodimer with M r 38,000 per subunit (SsNOX38) containing 1 FAD molecule/subunit. It oxidizes NADH and, less efficiently, NADPH with the formation of hydr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ed2e34ef98134ddb98e8b1523bac955
https://doi.org/10.1074/jbc.275.2.895
https://doi.org/10.1074/jbc.275.2.895
Publikováno v:
Journal of Thermal Analysis and Calorimetry. 61:363-368
The thermodynamic stability of pancreatic ribonuclease B (RNase B), which possesses identical protein structure of pancreatic ribonuclease A (RNase A), but differs by the presence of a carbohydrate chain attached to Asn 34, was studied by means of di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8b261505685505b685f82c53985c628a
https://doi.org/10.1023/a:1010101030232
https://doi.org/10.1023/a:1010101030232
Publikováno v:
International Journal of Biological Macromolecules. 26:45-53
In this study the pH dependence of the thermal stability of Sso7d from Sulfolobus solfataricus is analyzed. This small globular protein of 63 residues shows a very marked dependence of thermal stability on pH: the denaturation temperature passes from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a21454d8f28d4224a4a7de4be5188b26
https://doi.org/10.1016/s0141-8130(99)00059-8
https://doi.org/10.1016/s0141-8130(99)00059-8
Publikováno v:
Journal of Thermal Analysis and Calorimetry. 57:329-341
In this paper we try to perform a thermodynamic analysis of the temperature-induced transition from the molten globule to the unfolded state of globular proteins. A series of calorimetric investigations showed that this process is not associated with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fc56f1d520142b00ccd2235bf984687b
https://doi.org/10.1023/a:1010193909427
https://doi.org/10.1023/a:1010193909427
Autor:
Francesca Catanzano, B. de Paola, Mauro Rossi, Roberto Nucci, Sabato D'Auria, Giampaolo Barone, Giuseppe Graziano
Publikováno v:
Biochemistry. 37:14484-14490
Guanidine-induced denaturation of Sulfolobus solfataricus beta-glycosidase expressed in Escherichia coli, Sbetagly, was investigated at pH 6.5 and 25 degreesC by means of circular dichroism and fluorescence measurements. The process proved reversible
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d584b5f0bd3612ff55fff4d79c938589
https://doi.org/10.1021/bi980490w
https://doi.org/10.1021/bi980490w
Publikováno v:
Biochemistry. 37:10493-10498
Sso7d from the thermoacidophilic archaebacterium Sulfolobus solfataricus is a small globular protein with a known three-dimensional structure. Inspection of the structure reveals that Phe31 is a member of the aromatic cluster forming the protein hydr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a43a01038d141007f6291fc1b8d16c1
https://doi.org/10.1021/bi972994k
https://doi.org/10.1021/bi972994k