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The role of the N‐terminal domain of photoactive yellow protein in the transient partial unfolding during signalling state formation
Author(s) -
van der Horst Michael A,
van Stokkum Ivo H,
Crielaard Wim,
Hellingwerf Klaas J
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02427-9
Subject(s) - chromophore , chemistry , protonation , terminal (telecommunication) , ground state , domain (mathematical analysis) , cooperativity , titration , pas domain , crystallography , biophysics , photochemistry , biochemistry , gene , biology , physics , transcription factor , organic chemistry , ion , telecommunications , mathematical analysis , mathematics , quantum mechanics , computer science
It is shown that the N‐terminal domain of photoactive yellow protein (PYP), which appears relatively independently folded in the ground state of the protein, plays a key role in the transient unfolding during signalling state formation: genetic truncation of the N‐terminal domain of PYP significantly decreases the extent of cooperativity of the titration curve that describes chromophore protonation in the ground state of PYP, which is in agreement with the notion that the N‐terminal domain is linked through a hydrogen‐bonding network with the chromophore‐containing domain of the protein. Furthermore, deletion of the N‐terminal domain completely abolishes the non‐linearity of the Arrhenius plot of the rate of ground state recovery.