2022
Seeing the invisible – Study of transiently formed protein conformation found in domain 1.1 of bacterial transcription factor
TUŽINČIN, Dávid; Pavel KADEŘÁVEK; Petr PADRTA a Lukáš ŽÍDEKZákladní údaje
Originální název
Seeing the invisible – Study of transiently formed protein conformation found in domain 1.1 of bacterial transcription factor
Autoři
TUŽINČIN, Dávid (703 Slovensko, domácí); Pavel KADEŘÁVEK (203 Česká republika, garant); Petr PADRTA (203 Česká republika) a Lukáš ŽÍDEK (203 Česká republika)
Vydání
XVIII Discussions in Structural Molecular Biology and 5th User Meeting of CIISB (Czech Infrastructure for Integrative Structural Biology), 2022
Další údaje
Jazyk
angličtina
Typ výsledku
Prezentace na konferencích
Obor
10609 Biochemical research methods
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Kód RIV
RIV/00216224:14310/22:00126954
Organizační jednotka
Přírodovědecká fakulta
Klíčová slova anglicky
NMR; sigmaA; Bacillus subtilis; region 1.1; protein dynamics
Změněno: 13. 6. 2023 13:44, Mgr. Dávid Tužinčin
Anotace
V originále
Biomolecules undergo a variety of motions at various timescales. Motions at microsecond to millisecond timescales are often associated with transitions between ground states and higher energy states. Methods of structural biology allow detailed characterization of ground state structure and dynamics. However, the studies of higher energy state conformations are more difficult, because of their low occupancies and short lifetimes. Due to this fact, studies of excited states are often omitted. But nuclear magnetic resonance provides methods to investigate motions associated with these transitions and structures of excited states. In here, we investigate such conformational exchange, between well-defined ground state and transiently formed excited state which has been detected in domain 1.1 of primary sigma transcription factor from Bacillus subtillis. Sigma factor is essential for initiating the process of transcription, a fundamental cellular process. With the use of relaxation dispersion experiments we obtained structural information about orientations of bond vectors and secondary structure propensities within the excited state. Our results suggest that the excited state (populated only about 3% in the solution at 25 °C) has significantly lower propensity to form a stable secondary structure in the regions of helix I and helix III compared to the ground state.
Návaznosti
EF18_070/0009846, projekt VaV |
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GJ18-04197Y, projekt VaV |
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LM2018127, projekt VaV |
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MUNI/A/1467/2021, interní kód MU |
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