ArticleBiophysical journal2006
Conformational changes of PYP monitored by diffusion coefficient: effect of N-terminal alpha-helices.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Reversible molecular motional switch based on circular photoactive protein oligomers exhibits unexpected photo-induced contraction.Cell reports. Physical science · 2021Article
- Effect of Hydrated Ionic Liquid on Photocycle and Dynamics of Photoactive Yellow Protein.Molecules (Basel, Switzerland) · 2021Article
- Picosecond Photobiology: Watching a Signaling Protein Function in Real Time via Time-Resolved Small- and Wide-Angle X-ray Scattering.Journal of the American Chemical Society · 2016Article
- Small fluorescence-activating and absorption-shifting tag for tunable protein imaging in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- A circularly permuted photoactive yellow protein as a scaffold for photoswitch design.Biochemistry · 2013Article
- Light-induced conformational changes in full-length Arabidopsis thaliana cryptochrome.Journal of molecular biology · 2011Article
- Conformational changes in the N-terminal region of photoactive yellow protein: a time-resolved diffusion study.Biophysical journal · 2008Article
- Characterization of the solution structure of the M intermediate of photoactive yellow protein using high-angle solution x-ray scattering.Biophysical journal · 2007Article
- Photoreverse reaction dynamics of octopus rhodopsin.Biophysical journal · 2007Article
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5 authors.
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Abstract
Conformational changes in the light illuminated intermediate (pB) of photoactive yellow protein (PYP) were studied from a viewpoint of the diffusion coefficient (D) change of several N-truncated PYPs, which lacked the N-terminal 6, 15, or 23 amino acid residues (T6, T15, and T23, respectively). For intact PYP (i-PYP), D of pB (D(pB)) was approximately 11% lower than that (D(pG)) of the ground state (pG) species. The difference in D (D(pG) - D(pB)) decreased upon cleavage of the N-terminal region in the order of i-PYP>T6>T15>T23. This trend clearly showed that conformational change in the N-terminal group is the main reason for the slower diffusion of pB. This slower diffusion was interpreted in terms of the unfolding of the two alpha-helices in the N-terminal region, increasing the intermolecular interactions due to hydrogen bonding with water molecules. The increase in friction per one residue by the unfolding of the alpha-helix was estimated to be 0.3 x 10(-12) kg/s. The conformational change in the N-terminal group upon photoillumination is discussed.
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