Transcription is essential process for cell life, which is
precisely regulated. In bacteria, this process is mediated
through enzyme RNA polymerase. In order to initiate
transcription additional protein is necessary, the sigma
subunit. Its domain, sigma1.1, is responsible for the
autoinhibition of sigma in the free state and in the early
stages of transcription initiation sigma1.1 occupies the DNA
binding channel. This work focuses on domain 1.1 of
\textit{Bacillus subtilis}. In domain 1.1, highly imbalanced
conformational exchange was detected. Due to the possibility of
this conformational exchange being significant during
transcription, the low populated conformation was studied.
Within this work, high-field nuclear magnetic resonance was
used to study conformational process at atomic level
resolution. Using advanced relaxation dispersion experiments,
structural information about the orientation and secondary
structure of the excited state was obtained.