Structural characterisation and comparison of the native and A-states of equine lysozyme

Morozova‐Roche, Ludmilla A.; Haynie, Donald T.; Emelyanenko, V. I.; Dael, H. Van; Dobson, Christopher M.

doi:10.1006/jmbi.1997.0996

Cited by 74 publications

(116 citation statements)

References 85 publications

(124 reference statements)

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“…In addition, the native-like tertiary structure was found to be retained relatively well, even in the non-native state at pH 2.0 (Fig. 1D), which was similar to the molten globule state of equine lysozyme (28). Thus, we conclude that the nonnative state at pH 2.0 can be considered as an acid-induced molten globule state (A-state).…”

Section: Resultsmentioning

confidence: 57%

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Acid-induced Molten Globule State of a Prion Protein

Honda

Yamaguchi

Kuwata

2014

Journal of Biological Chemistry

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Background:The oligomerization mechanism of a prion protein is not fully understood. Results:We found an acid-induced molten globule state (A-state) as a pre-oligomer state, in which the Strand 1-Helix 1-Strand 2 segment was unfolded. Conclusion: The A-state formation is the initial step of the oligomerization. Significance: This work may offer a clue for understanding the prion's pathogenic conversion mechanism.

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Section: Resultsmentioning

confidence: 57%

“…1D) similar to the molten globule state of equine lysozyme (28). In the molten globule state of equine lysozyme, the native-like tertiary structure was located in the region where the backbone protection factors are relatively high.…”

Section: Discussionmentioning

confidence: 81%

Acid-induced Molten Globule State of a Prion Protein

Honda

Yamaguchi

Kuwata

2014

Journal of Biological Chemistry

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“…EL forms a wide range of partially folded states under equilibrium conditions similar to these of -lactalbumins [16,3,17,18]. However, EL molten globule is much more structured compared to the "classical" molten globules of α-lactalbumins, possessing an extended native-like hydrophobic core stabilised by interactions between three major α-helices (A, B and D-helices) in the α-domain [17,18]. Like c-type lysozymes, during refolding kinetics EL forms an ensemble of well-defined transient kinetic intermediates, possessing very persistent structures [19].…”

Section: Equine Lysozyme (El) As a Structural Homologue Of α-Lactalbuminmentioning

confidence: 99%

“…The CIDNP spectra of the native EL at several pH 4.5, 6.9 and 9.0 are well-resolved and were assigned by comparison with NMR chemical shifts [17,18,22]. ELOA and EL molten display less resolved CIDNP spectra, consistent with their millisecond conformational fluctuations, although it is still straight forward to distinguish tyrosine and tryptophan/histidine residues based on their emissive (negative) and absorptive (positive) polarizations, respectively.…”

Section: El Conformation In Eloamentioning

confidence: 99%

“…The calciumbinding usually increases the protein stability against denaturing treatments, however in the case of EL, the significantly lower stability and cooperatively was observed compared to non-calcium-binding lysozymes even in its holo-form, while in the apo-form its thermodynamic stability is closer of -lactalbumins than to c-type lysozymes [15,16]. EL forms a wide range of partially folded states under equilibrium conditions similar to these of -lactalbumins [16,3,17,18]. However, EL molten globule is much more structured compared to the "classical" molten globules of α-lactalbumins, possessing an extended native-like hydrophobic core stabilised by interactions between three major α-helices (A, B and D-helices) in the α-domain [17,18].…”

Section: Equine Lysozyme (El) As a Structural Homologue Of α-Lactalbuminmentioning

confidence: 99%

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Structural Origin of ELOA Toxicity – Implication for HAMLET-Type Protein Complexes with Oleic Acid

Vukojević¹,

Morozova‐Roche²

2012

Lipoproteins - Role in Health and Diseases

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Hydrogen exchange study of canine milk lysozyme: Stabilization mechanism of the molten globule

Kobashigawa¹,

Demura²,

Koshiba³

et al. 2000

Proteins

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The native state 1H, 15N resonance assignment of 123 of the 128 nonproline residues of canine milk lysozyme has enabled measurements of the amide hydrogen exchange of over 70 amide hydrogens in the molten globule state. To elucidate the mechanism of protein folding, the molten globule state has been studied as a model of the folding intermediate state. Lysozyme and α‐lactalbumin are homologous to each other, but their equilibrium unfolding mechanisms differ. Generally, the folding mechanism of lysozyme obeys a two‐state model, whereas that of α‐lactalbumin follows a three‐state model. Exceptions to this rule are equine and canine milk lysozymes, which exhibit a partially unfolded state during the equilibrium unfolding; this state resembles the molten globule state of α‐lactalbumin but with extreme stability. Study of the molten globules of α‐lactalbumin and equine milk lysozyme showed that the stabilities of their α‐helices are similar, despite the differences in the thermodynamic stability of their molten globule states. On the other hand, our hydrogen exchange study of the molten globule of canine milk lysozyme showed that the α‐helices are more stabilized than in α‐lactalbumin or equine milk lysozyme and that this enhanced stability is caused by the strengthened cooperative interaction between secondary structure elements. Thus, our results underscore the importance of the cooperative interaction in the stability of the molten globule state. Proteins 2000;40:579–589. © 2000 Wiley‐Liss, Inc.

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Structural characterisation and comparison of the native and A-states of equine lysozyme

Cited by 74 publications

References 85 publications

Acid-induced Molten Globule State of a Prion Protein

Acid-induced Molten Globule State of a Prion Protein

Structural Origin of ELOA Toxicity – Implication for HAMLET-Type Protein Complexes with Oleic Acid

Hydrogen exchange study of canine milk lysozyme: Stabilization mechanism of the molten globule

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