light-induced Fourier transform infrared (FTIR) difference spectroscopy

The N-terminal and C-terminal helices of phototropin LOV2 domains are necessary for allosteric regulation of the phototropin kinase domain and may support signal integration of LOV1 and LOV2 domains.

It also suggests that the N- and C-terminal helices of phot-LOV2 domains are necessary for allosteric regulation of the phototropin kinase domain and may provide a basis for signal integration of LOV1 and LOV2 domains in phototropins.

The N-terminal and C-terminal helices of phototropin LOV2 domains are necessary for allosteric regulation of the phototropin kinase domain and may support signal integration of LOV1 and LOV2 domains.

It also suggests that the N- and C-terminal helices of phot-LOV2 domains are necessary for allosteric regulation of the phototropin kinase domain and may provide a basis for signal integration of LOV1 and LOV2 domains in phototropins.

The N-terminal and C-terminal helices of phototropin LOV2 domains are necessary for allosteric regulation of the phototropin kinase domain and may support signal integration of LOV1 and LOV2 domains.

It also suggests that the N- and C-terminal helices of phot-LOV2 domains are necessary for allosteric regulation of the phototropin kinase domain and may provide a basis for signal integration of LOV1 and LOV2 domains in phototropins.

The N-terminal and C-terminal helices of phototropin LOV2 domains are necessary for allosteric regulation of the phototropin kinase domain and may support signal integration of LOV1 and LOV2 domains.

It also suggests that the N- and C-terminal helices of phot-LOV2 domains are necessary for allosteric regulation of the phototropin kinase domain and may provide a basis for signal integration of LOV1 and LOV2 domains in phototropins.

The N-terminal and C-terminal helices of phototropin LOV2 domains are necessary for allosteric regulation of the phototropin kinase domain and may support signal integration of LOV1 and LOV2 domains.

It also suggests that the N- and C-terminal helices of phot-LOV2 domains are necessary for allosteric regulation of the phototropin kinase domain and may provide a basis for signal integration of LOV1 and LOV2 domains in phototropins.

The conformational changes in full-length phototropin LOV domains may be smaller than previously assumed, and full unfolding of the Jα helix in AsLOV2 constructs with short A'α helices may be a truncation artifact.

These results are different from shorter constructs, indicating that the conformational changes in full-length phototropin LOV domains might not be as large as previously assumed, and that the well-characterized full unfolding of the Jα helix in AsLOV2 with short A'α helices may be considered a truncation artifact.

The conformational changes in full-length phototropin LOV domains may be smaller than previously assumed, and full unfolding of the Jα helix in AsLOV2 constructs with short A'α helices may be a truncation artifact.

These results are different from shorter constructs, indicating that the conformational changes in full-length phototropin LOV domains might not be as large as previously assumed, and that the well-characterized full unfolding of the Jα helix in AsLOV2 with short A'α helices may be considered a truncation artifact.

The conformational changes in full-length phototropin LOV domains may be smaller than previously assumed, and full unfolding of the Jα helix in AsLOV2 constructs with short A'α helices may be a truncation artifact.

These results are different from shorter constructs, indicating that the conformational changes in full-length phototropin LOV domains might not be as large as previously assumed, and that the well-characterized full unfolding of the Jα helix in AsLOV2 with short A'α helices may be considered a truncation artifact.

The conformational changes in full-length phototropin LOV domains may be smaller than previously assumed, and full unfolding of the Jα helix in AsLOV2 constructs with short A'α helices may be a truncation artifact.

These results are different from shorter constructs, indicating that the conformational changes in full-length phototropin LOV domains might not be as large as previously assumed, and that the well-characterized full unfolding of the Jα helix in AsLOV2 with short A'α helices may be considered a truncation artifact.

The conformational changes in full-length phototropin LOV domains may be smaller than previously assumed, and full unfolding of the Jα helix in AsLOV2 constructs with short A'α helices may be a truncation artifact.

These results are different from shorter constructs, indicating that the conformational changes in full-length phototropin LOV domains might not be as large as previously assumed, and that the well-characterized full unfolding of the Jα helix in AsLOV2 with short A'α helices may be considered a truncation artifact.

In phototropin LOV2 domains, blue light illumination leads to covalent bond formation between protein and flavin that induces dissociation and unfolding of the C-terminal Jα helix and the N-terminal A'α helix.

In the second LOV domain of phototropins, called LOV2 domains, blue light illumination leads to covalent bond formation between protein and flavin that induces the dissociation and unfolding of a C-terminally attached α helix (Jα) and the N-terminal helix (A'α).

In phototropin LOV2 domains, blue light illumination leads to covalent bond formation between protein and flavin that induces dissociation and unfolding of the C-terminal Jα helix and the N-terminal A'α helix.

In the second LOV domain of phototropins, called LOV2 domains, blue light illumination leads to covalent bond formation between protein and flavin that induces the dissociation and unfolding of a C-terminally attached α helix (Jα) and the N-terminal helix (A'α).

In phototropin LOV2 domains, blue light illumination leads to covalent bond formation between protein and flavin that induces dissociation and unfolding of the C-terminal Jα helix and the N-terminal A'α helix.

In the second LOV domain of phototropins, called LOV2 domains, blue light illumination leads to covalent bond formation between protein and flavin that induces the dissociation and unfolding of a C-terminally attached α helix (Jα) and the N-terminal helix (A'α).

In phototropin LOV2 domains, blue light illumination leads to covalent bond formation between protein and flavin that induces dissociation and unfolding of the C-terminal Jα helix and the N-terminal A'α helix.

In the second LOV domain of phototropins, called LOV2 domains, blue light illumination leads to covalent bond formation between protein and flavin that induces the dissociation and unfolding of a C-terminally attached α helix (Jα) and the N-terminal helix (A'α).

In phototropin LOV2 domains, blue light illumination leads to covalent bond formation between protein and flavin that induces dissociation and unfolding of the C-terminal Jα helix and the N-terminal A'α helix.

In the second LOV domain of phototropins, called LOV2 domains, blue light illumination leads to covalent bond formation between protein and flavin that induces the dissociation and unfolding of a C-terminally attached α helix (Jα) and the N-terminal helix (A'α).

Deletion of the A'α helix abolishes light-induced unfolding of the Jα helix in AsLOV2.

Deletion of the A'α helix abolishes the light-induced unfolding of Jα

Deletion of the A'α helix abolishes light-induced unfolding of the Jα helix in AsLOV2.

Deletion of the A'α helix abolishes the light-induced unfolding of Jα

Deletion of the A'α helix abolishes light-induced unfolding of the Jα helix in AsLOV2.

Deletion of the A'α helix abolishes the light-induced unfolding of Jα

Deletion of the A'α helix abolishes light-induced unfolding of the Jα helix in AsLOV2.

Deletion of the A'α helix abolishes the light-induced unfolding of Jα

Deletion of the A'α helix abolishes light-induced unfolding of the Jα helix in AsLOV2.

Deletion of the A'α helix abolishes the light-induced unfolding of Jα

Extensions of the A'α helix attenuate the light-induced structural change of the Jα helix in AsLOV2.

whereas extensions of the A'α helix lead to an attenuated structural change of Jα

Extensions of the A'α helix attenuate the light-induced structural change of the Jα helix in AsLOV2.

whereas extensions of the A'α helix lead to an attenuated structural change of Jα

Extensions of the A'α helix attenuate the light-induced structural change of the Jα helix in AsLOV2.

whereas extensions of the A'α helix lead to an attenuated structural change of Jα

Extensions of the A'α helix attenuate the light-induced structural change of the Jα helix in AsLOV2.

whereas extensions of the A'α helix lead to an attenuated structural change of Jα

Extensions of the A'α helix attenuate the light-induced structural change of the Jα helix in AsLOV2.

whereas extensions of the A'α helix lead to an attenuated structural change of Jα

The C4=O stretching bands of the FAD isoalloxazine ring were induced at the same frequency and with the same band intensity in YcgF-Full and YcgF-BLUF spectra.

the bands for the C4=O stretching of a FAD isoalloxazine ring were induced at the same frequency with the same band intensity in the spectra for YcgF-Full and YcgF-BLUF

The C4=O stretching bands of the FAD isoalloxazine ring were induced at the same frequency and with the same band intensity in YcgF-Full and YcgF-BLUF spectra.

the bands for the C4=O stretching of a FAD isoalloxazine ring were induced at the same frequency with the same band intensity in the spectra for YcgF-Full and YcgF-BLUF

The C4=O stretching bands of the FAD isoalloxazine ring were induced at the same frequency and with the same band intensity in YcgF-Full and YcgF-BLUF spectra.

the bands for the C4=O stretching of a FAD isoalloxazine ring were induced at the same frequency with the same band intensity in the spectra for YcgF-Full and YcgF-BLUF

The C4=O stretching bands of the FAD isoalloxazine ring were induced at the same frequency and with the same band intensity in YcgF-Full and YcgF-BLUF spectra.

the bands for the C4=O stretching of a FAD isoalloxazine ring were induced at the same frequency with the same band intensity in the spectra for YcgF-Full and YcgF-BLUF

The C4=O stretching bands of the FAD isoalloxazine ring were induced at the same frequency and with the same band intensity in YcgF-Full and YcgF-BLUF spectra.

the bands for the C4=O stretching of a FAD isoalloxazine ring were induced at the same frequency with the same band intensity in the spectra for YcgF-Full and YcgF-BLUF

The C4=O stretching bands of the FAD isoalloxazine ring were induced at the same frequency and with the same band intensity in YcgF-Full and YcgF-BLUF spectra.

the bands for the C4=O stretching of a FAD isoalloxazine ring were induced at the same frequency with the same band intensity in the spectra for YcgF-Full and YcgF-BLUF

The C4=O stretching bands of the FAD isoalloxazine ring were induced at the same frequency and with the same band intensity in YcgF-Full and YcgF-BLUF spectra.

the bands for the C4=O stretching of a FAD isoalloxazine ring were induced at the same frequency with the same band intensity in the spectra for YcgF-Full and YcgF-BLUF

The C4=O stretching bands of the FAD isoalloxazine ring were induced at the same frequency and with the same band intensity in YcgF-Full and YcgF-BLUF spectra.

the bands for the C4=O stretching of a FAD isoalloxazine ring were induced at the same frequency with the same band intensity in the spectra for YcgF-Full and YcgF-BLUF

The C4=O stretching bands of the FAD isoalloxazine ring were induced at the same frequency and with the same band intensity in YcgF-Full and YcgF-BLUF spectra.

the bands for the C4=O stretching of a FAD isoalloxazine ring were induced at the same frequency with the same band intensity in the spectra for YcgF-Full and YcgF-BLUF

The C4=O stretching bands of the FAD isoalloxazine ring were induced at the same frequency and with the same band intensity in YcgF-Full and YcgF-BLUF spectra.

the bands for the C4=O stretching of a FAD isoalloxazine ring were induced at the same frequency with the same band intensity in the spectra for YcgF-Full and YcgF-BLUF

Escherichia coli YcgF is a BLUF protein composed of an N-terminal BLUF domain and a C-terminal EAL domain.

The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain.

Escherichia coli YcgF is a BLUF protein composed of an N-terminal BLUF domain and a C-terminal EAL domain.

The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain.

Escherichia coli YcgF is a BLUF protein composed of an N-terminal BLUF domain and a C-terminal EAL domain.

The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain.

Escherichia coli YcgF is a BLUF protein composed of an N-terminal BLUF domain and a C-terminal EAL domain.

The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain.

Escherichia coli YcgF is a BLUF protein composed of an N-terminal BLUF domain and a C-terminal EAL domain.

The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain.

Escherichia coli YcgF is a BLUF protein composed of an N-terminal BLUF domain and a C-terminal EAL domain.

The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain.

Escherichia coli YcgF is a BLUF protein composed of an N-terminal BLUF domain and a C-terminal EAL domain.

The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain.

Escherichia coli YcgF is a BLUF protein composed of an N-terminal BLUF domain and a C-terminal EAL domain.

The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain.

Escherichia coli YcgF is a BLUF protein composed of an N-terminal BLUF domain and a C-terminal EAL domain.

The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain.

Escherichia coli YcgF is a BLUF protein composed of an N-terminal BLUF domain and a C-terminal EAL domain.

The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.

The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.

The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.

The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.

The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.

The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.

The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.

The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.

The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.

The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.

The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.

The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.

The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.

The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.

The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.

The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.

The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.

The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.

The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.

The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.

The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.

The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.

The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.

The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.

The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.

The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.

The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.

The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.

The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.

The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.

The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.

The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.

The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.

The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.

The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.

YcgF-Full and YcgF-BLUF showed identical dark-state flavin UV-visible absorption spectra and identical kinetics of relaxation from the light-induced signaling state to the dark state.

YcgF-Full and YcgF-BLUF showed identical UV-visible absorption spectra of flavin in the dark state and a light-induced absorption red shift for the signaling state, which relaxed to the dark state showing identical kinetics.

YcgF-Full and YcgF-BLUF showed identical dark-state flavin UV-visible absorption spectra and identical kinetics of relaxation from the light-induced signaling state to the dark state.

YcgF-Full and YcgF-BLUF showed identical UV-visible absorption spectra of flavin in the dark state and a light-induced absorption red shift for the signaling state, which relaxed to the dark state showing identical kinetics.

YcgF-Full and YcgF-BLUF showed identical dark-state flavin UV-visible absorption spectra and identical kinetics of relaxation from the light-induced signaling state to the dark state.

YcgF-Full and YcgF-BLUF showed identical UV-visible absorption spectra of flavin in the dark state and a light-induced absorption red shift for the signaling state, which relaxed to the dark state showing identical kinetics.

YcgF-Full and YcgF-BLUF showed identical dark-state flavin UV-visible absorption spectra and identical kinetics of relaxation from the light-induced signaling state to the dark state.

YcgF-Full and YcgF-BLUF showed identical UV-visible absorption spectra of flavin in the dark state and a light-induced absorption red shift for the signaling state, which relaxed to the dark state showing identical kinetics.

YcgF-Full and YcgF-BLUF showed identical dark-state flavin UV-visible absorption spectra and identical kinetics of relaxation from the light-induced signaling state to the dark state.

YcgF-Full and YcgF-BLUF showed identical UV-visible absorption spectra of flavin in the dark state and a light-induced absorption red shift for the signaling state, which relaxed to the dark state showing identical kinetics.

YcgF-Full and YcgF-BLUF showed identical dark-state flavin UV-visible absorption spectra and identical kinetics of relaxation from the light-induced signaling state to the dark state.

YcgF-Full and YcgF-BLUF showed identical UV-visible absorption spectra of flavin in the dark state and a light-induced absorption red shift for the signaling state, which relaxed to the dark state showing identical kinetics.

YcgF-Full and YcgF-BLUF showed identical dark-state flavin UV-visible absorption spectra and identical kinetics of relaxation from the light-induced signaling state to the dark state.

YcgF-Full and YcgF-BLUF showed identical UV-visible absorption spectra of flavin in the dark state and a light-induced absorption red shift for the signaling state, which relaxed to the dark state showing identical kinetics.

YcgF-Full and YcgF-BLUF showed identical dark-state flavin UV-visible absorption spectra and identical kinetics of relaxation from the light-induced signaling state to the dark state.

YcgF-Full and YcgF-BLUF showed identical UV-visible absorption spectra of flavin in the dark state and a light-induced absorption red shift for the signaling state, which relaxed to the dark state showing identical kinetics.

YcgF-Full and YcgF-BLUF showed identical dark-state flavin UV-visible absorption spectra and identical kinetics of relaxation from the light-induced signaling state to the dark state.

YcgF-Full and YcgF-BLUF showed identical UV-visible absorption spectra of flavin in the dark state and a light-induced absorption red shift for the signaling state, which relaxed to the dark state showing identical kinetics.

YcgF-Full and YcgF-BLUF showed identical dark-state flavin UV-visible absorption spectra and identical kinetics of relaxation from the light-induced signaling state to the dark state.

YcgF-Full and YcgF-BLUF showed identical UV-visible absorption spectra of flavin in the dark state and a light-induced absorption red shift for the signaling state, which relaxed to the dark state showing identical kinetics.

The full-length-specific protein bands are discussed as being predominantly attributable to structural changes in the C-terminal EAL domain triggered by light excitation of the N-terminal BLUF domain.

The possibility that full-length-specific protein bands are predominantly ascribed to structural changes of the C-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminal BLUF domain is discussed.

The full-length-specific protein bands are discussed as being predominantly attributable to structural changes in the C-terminal EAL domain triggered by light excitation of the N-terminal BLUF domain.

The possibility that full-length-specific protein bands are predominantly ascribed to structural changes of the C-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminal BLUF domain is discussed.

The full-length-specific protein bands are discussed as being predominantly attributable to structural changes in the C-terminal EAL domain triggered by light excitation of the N-terminal BLUF domain.

The possibility that full-length-specific protein bands are predominantly ascribed to structural changes of the C-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminal BLUF domain is discussed.

The full-length-specific protein bands are discussed as being predominantly attributable to structural changes in the C-terminal EAL domain triggered by light excitation of the N-terminal BLUF domain.

The possibility that full-length-specific protein bands are predominantly ascribed to structural changes of the C-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminal BLUF domain is discussed.

The full-length-specific protein bands are discussed as being predominantly attributable to structural changes in the C-terminal EAL domain triggered by light excitation of the N-terminal BLUF domain.

The possibility that full-length-specific protein bands are predominantly ascribed to structural changes of the C-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminal BLUF domain is discussed.

The full-length-specific protein bands are discussed as being predominantly attributable to structural changes in the C-terminal EAL domain triggered by light excitation of the N-terminal BLUF domain.

The possibility that full-length-specific protein bands are predominantly ascribed to structural changes of the C-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminal BLUF domain is discussed.

The full-length-specific protein bands are discussed as being predominantly attributable to structural changes in the C-terminal EAL domain triggered by light excitation of the N-terminal BLUF domain.

The possibility that full-length-specific protein bands are predominantly ascribed to structural changes of the C-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminal BLUF domain is discussed.

The full-length-specific protein bands are discussed as being predominantly attributable to structural changes in the C-terminal EAL domain triggered by light excitation of the N-terminal BLUF domain.

The possibility that full-length-specific protein bands are predominantly ascribed to structural changes of the C-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminal BLUF domain is discussed.

The full-length-specific protein bands are discussed as being predominantly attributable to structural changes in the C-terminal EAL domain triggered by light excitation of the N-terminal BLUF domain.

The possibility that full-length-specific protein bands are predominantly ascribed to structural changes of the C-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminal BLUF domain is discussed.

The full-length-specific protein bands are discussed as being predominantly attributable to structural changes in the C-terminal EAL domain triggered by light excitation of the N-terminal BLUF domain.

The possibility that full-length-specific protein bands are predominantly ascribed to structural changes of the C-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminal BLUF domain is discussed.

At medium-low temperatures, the YcgF-Full FTIR spectrum resembled the YcgF-BLUF spectrum because protein bands were selectively suppressed.

the YcgF-Full spectrum resembled that of the YcgF-BLUF when illuminated at medium-low temperatures because of the selective suppression of protein bands

At medium-low temperatures, the YcgF-Full FTIR spectrum resembled the YcgF-BLUF spectrum because protein bands were selectively suppressed.

the YcgF-Full spectrum resembled that of the YcgF-BLUF when illuminated at medium-low temperatures because of the selective suppression of protein bands

At medium-low temperatures, the YcgF-Full FTIR spectrum resembled the YcgF-BLUF spectrum because protein bands were selectively suppressed.

the YcgF-Full spectrum resembled that of the YcgF-BLUF when illuminated at medium-low temperatures because of the selective suppression of protein bands

At medium-low temperatures, the YcgF-Full FTIR spectrum resembled the YcgF-BLUF spectrum because protein bands were selectively suppressed.

the YcgF-Full spectrum resembled that of the YcgF-BLUF when illuminated at medium-low temperatures because of the selective suppression of protein bands

At medium-low temperatures, the YcgF-Full FTIR spectrum resembled the YcgF-BLUF spectrum because protein bands were selectively suppressed.

the YcgF-Full spectrum resembled that of the YcgF-BLUF when illuminated at medium-low temperatures because of the selective suppression of protein bands

At medium-low temperatures, the YcgF-Full FTIR spectrum resembled the YcgF-BLUF spectrum because protein bands were selectively suppressed.

the YcgF-Full spectrum resembled that of the YcgF-BLUF when illuminated at medium-low temperatures because of the selective suppression of protein bands

At medium-low temperatures, the YcgF-Full FTIR spectrum resembled the YcgF-BLUF spectrum because protein bands were selectively suppressed.

the YcgF-Full spectrum resembled that of the YcgF-BLUF when illuminated at medium-low temperatures because of the selective suppression of protein bands

At medium-low temperatures, the YcgF-Full FTIR spectrum resembled the YcgF-BLUF spectrum because protein bands were selectively suppressed.

the YcgF-Full spectrum resembled that of the YcgF-BLUF when illuminated at medium-low temperatures because of the selective suppression of protein bands

At medium-low temperatures, the YcgF-Full FTIR spectrum resembled the YcgF-BLUF spectrum because protein bands were selectively suppressed.

the YcgF-Full spectrum resembled that of the YcgF-BLUF when illuminated at medium-low temperatures because of the selective suppression of protein bands

At medium-low temperatures, the YcgF-Full FTIR spectrum resembled the YcgF-BLUF spectrum because protein bands were selectively suppressed.

the YcgF-Full spectrum resembled that of the YcgF-BLUF when illuminated at medium-low temperatures because of the selective suppression of protein bands

The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.

The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.

Source: Light Induced Structural Changes of a Full-length Protein and Its BLUF Domain in YcgF(Blrp), a Blue-Light Sensing Protein That Uses FAD (BLUF)