Changes of structure and intramolecular mobility in the course of actin denaturation

Kuznetsova, Irina M.; Khaitlina, Sofia; Konditerov, S.N.; Surin, A.M.; Turoverov, Konstantin K.

doi:10.1016/0301-4622(88)85035-x

Cited by 38 publications

(55 citation statements)

References 8 publications

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“…However, we show that in this new structural state, the average Trp environment acquires an apparent increase in hydrophobicity. Kuznetsova et al (1988), working on tryptophan residues in actin, reported results similar to those reported here. These authors found that in spite of an increase of intramolecular mobility, heated actin still retains the asymmetrical microenvironment of the tryptophan residues.…”

Section: Resultssupporting

confidence: 80%

Thermal transitions in the structure of tubulin

Mozo-Villarías¹,

Morros

Andreu

1991

Eur Biophys J

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The environment of aromatic aminoacids in the thermal transition of brain tubulin has been studied by several spectroscopic techniques (Fourth Derivative, Difference Absorption, Fluorescence and Circular Dichroism), in order to study its denaturation. An irreversible, temperature-induced, structural transition was found at around 48 degrees C. In order to establish the relative degree of hydrophobicity of tubulin aromatic residues, before and after the thermal transition, difference and fourth derivative absorption spectra at different temperatures were compared with spectra of tyrosine and tryptophan model compounds in different media. It was found that at high temperatures, tubulin acquires a partially denatured stable state, with a significant amount of residual structure still preserved. This state is characterized by a general increase of the exposure of tyrosine residues to the medium, while the environment of tryptophans becomes more hydrophobic.

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Section: Resultssupporting

confidence: 80%

Thermal transitions in the structure of tubulin

Mozo-Villarías¹,

Morros

Andreu

1991

Eur Biophys J

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“…These data, taken together, provide evidence for high conformational coupling within the 'small' domain, which is responsible for interaction with many actin-binding proteins. The position of the intrinsic tryptophan residues in the focus of these transitions could explain the high sensitivity of tryptophan fluorescence to actin polymerization and modifications of the polypeptide chain [19,20].…”

Section: Discussionmentioning

confidence: 99%

Conformational changes in subdomain I of actin induced by proteolytic cleavage within the DNase I‐binding loop: energy transfer from tryptophan to AEDANS

et al. 1996

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Alteration of the actin polypeptide chain within the DNnse I-binding loop by cleavage with E. coli A2 protease or suhtilisin was shown to increase the efficiency of energy transfer from tryptophan residues to AEDANS attached to Cys-374. Analysis of structural and fluorescence data suggested that only two of four actin tryptophan residues, namely, Trp-340 and/or Trp-356, can he energy transfer donors. It was also found that labelling with AEDANS induces perturbations in the environment of the tryptophan residues, these perturbations being smaller in the cleaved actin. These changes are consistent with a shift of the C-terminal segment of actin monomer upon cleavage and confirm the existence of high conformational coupling between subdomains 1 and 2 of actin monomer. We also suggest that tryptophan residues 340 and/or 356 are located in the focus of this coupling.

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“…Therefore, in these two conformations the tryptophan residues participate in the high-frequency intramolecular motions whose rotational relaxation time is much shorter than the lifetime of the excited state. [28] Alternatively, these tryptophan residues may be involved in the intramolecular mobility on the nanosecond time scale whose rotational relaxation time does not depend on solvent viscosity. [29] Finally, the fact that 1/r ' 0p.f.…”

Section: Of Its Maximal Value)mentioning

confidence: 99%

Partially Folded Conformations in the Folding Pathway of Bovine Carbonic Anhydrase II: A Fluorescence Spectroscopic Analysis

et al. 2001

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GdmCl-, urea-, and pH-induced unfolding pathways of bovine carbonic anhydrase II have been analyzed by using changes induced by different denaturing agents in intensity, anisotropy, life time, and parameter A value of intrinsic fluorescence as well as intensity and life time of ANS (ammonium salt of 8-anilinonaphthalene-1-sulfonic acid) fluorescence. The formation of several stable unfolding intermediates, some of which were not observed previously, has been established. This was further confirmed by representation of fluorescence data in terms of a "phase diagram", that is, I(lambda1) versus I(lambda2) dependence, where I(lambda1) and I(lambda2) are the fluorescence intensity values measured at wavelengths lambda(1) and lambda(2), respectively.

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Changes of structure and intramolecular mobility in the course of actin denaturation

Cited by 38 publications

References 8 publications

Thermal transitions in the structure of tubulin

Thermal transitions in the structure of tubulin

Conformational changes in subdomain I of actin induced by proteolytic cleavage within the DNase I‐binding loop: energy transfer from tryptophan to AEDANS

Partially Folded Conformations in the Folding Pathway of Bovine Carbonic Anhydrase II: A Fluorescence Spectroscopic Analysis

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