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@proceedings{2225861,
author = {Tužinčin, Dávid and Kadeřávek, Pavel and Padrta, Petr and Žídek, Lukáš},
booktitle = {XVIII Discussions in Structural Molecular Biology and 5th User Meeting of CIISB (Czech Infrastructure for Integrative Structural Biology)},
keywords = {NMR; sigmaA; Bacillus subtilis; region 1.1; protein dynamics},
language = {eng},
title = {Seeing the invisible – Study of transiently formed protein conformation found in domain 1.1 of bacterial transcription factor},
url = {https://www.xray.cz/setkani/abst2022/505.htm},
year = {2022}
}
TY - CONF
ID - 2225861
AU - Tužinčin, Dávid - Kadeřávek, Pavel - Padrta, Petr - Žídek, Lukáš
PY - 2022
TI - Seeing the invisible – Study of transiently formed protein conformation found in domain 1.1 of bacterial transcription factor
KW - NMR
KW - sigmaA
KW - Bacillus subtilis
KW - region 1.1
KW - protein dynamics
UR - https://www.xray.cz/setkani/abst2022/505.htm
N2 - 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.
ER -
TUŽINČIN, Dávid, Pavel KADEŘÁVEK, Petr PADRTA and Lukáš ŽÍDEK. Seeing the invisible – Study of transiently formed protein conformation found in domain 1.1 of bacterial transcription factor. In \textit{XVIII Discussions in Structural Molecular Biology and 5th User Meeting of CIISB (Czech Infrastructure for Integrative Structural Biology)}. 2022.
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