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Independent of their localization in protein the hydrophobic amino acid residues have no effect on the molten globule state of apomyoglobin and the disulfide bond on the surface of apomyoglobin stabilizes this intermediate state.

Melnik TN, Majorina MA, Larina DS, Kashparov IA, Samatova EN, Glukhov AS, Melnik BS - PLoS ONE (2014)

Bottom Line: In this study, we have investigated the effect of substitutions of hydrophobic amino acid residues in the hydrophobic core of protein and on its surface on a molten globule type intermediate state of apomyoglobin.It has been found that independent of their localization in protein, substitutions of hydrophobic amino acid residues do not affect the stability of the molten globule state of apomyoglobin.The result obtained allows us not only to conclude which mutations can have an effect on the intermediate state of the molten globule type, but also explains why the introduction of a disulfide bond (which seems to "strengthen" the protein) can result in destabilization of the protein native state of apomyoglobin.

View Article: PubMed Central - PubMed

Affiliation: Institute of Protein Research, RAS, Pushchino, Moscow Region, Russia.

ABSTRACT
At present it is unclear which interactions in proteins reveal the presence of intermediate states, their stability and formation rate. In this study, we have investigated the effect of substitutions of hydrophobic amino acid residues in the hydrophobic core of protein and on its surface on a molten globule type intermediate state of apomyoglobin. It has been found that independent of their localization in protein, substitutions of hydrophobic amino acid residues do not affect the stability of the molten globule state of apomyoglobin. It has been shown also that introduction of a disulfide bond on the protein surface can stabilize the molten globule state. However in the case of apomyoglobin, stabilization of the intermediate state leads to relative destabilization of the native state of apomyoglobin. The result obtained allows us not only to conclude which mutations can have an effect on the intermediate state of the molten globule type, but also explains why the introduction of a disulfide bond (which seems to "strengthen" the protein) can result in destabilization of the protein native state of apomyoglobin.

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Choice of mutations in apomyoglobin.Three-dimensional structure of myoglobin (PDB-code: 1BZP) is shown with band model (A) and with balls models (B). Hydrophobic amino acid residues selected to substitute analine (A) and hydrophilic amino acid residues (B) are shown in blue color.
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pone-0098645-g001: Choice of mutations in apomyoglobin.Three-dimensional structure of myoglobin (PDB-code: 1BZP) is shown with band model (A) and with balls models (B). Hydrophobic amino acid residues selected to substitute analine (A) and hydrophilic amino acid residues (B) are shown in blue color.

Mentions: The following amino acid residues have been selected in the hydrophobic core of apomyoglobin: V10, W14, I28, F33, L61, L76, I111, L115, L131, and L135. They are large hydrophobic amino acid residues located in different structural elements of apomyoglobin (Fig. 1). Earlier we investigated the effect of these residues on the rates of refolding and unfolding of the apomyoglobin structure [11]. In this study, we analyze only the influence of single substitutions of hydrophobic amino acid residues on the stability of the molten globule state of apomyoglobin.


Independent of their localization in protein the hydrophobic amino acid residues have no effect on the molten globule state of apomyoglobin and the disulfide bond on the surface of apomyoglobin stabilizes this intermediate state.

Melnik TN, Majorina MA, Larina DS, Kashparov IA, Samatova EN, Glukhov AS, Melnik BS - PLoS ONE (2014)

Choice of mutations in apomyoglobin.Three-dimensional structure of myoglobin (PDB-code: 1BZP) is shown with band model (A) and with balls models (B). Hydrophobic amino acid residues selected to substitute analine (A) and hydrophilic amino acid residues (B) are shown in blue color.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4043776&req=5

pone-0098645-g001: Choice of mutations in apomyoglobin.Three-dimensional structure of myoglobin (PDB-code: 1BZP) is shown with band model (A) and with balls models (B). Hydrophobic amino acid residues selected to substitute analine (A) and hydrophilic amino acid residues (B) are shown in blue color.
Mentions: The following amino acid residues have been selected in the hydrophobic core of apomyoglobin: V10, W14, I28, F33, L61, L76, I111, L115, L131, and L135. They are large hydrophobic amino acid residues located in different structural elements of apomyoglobin (Fig. 1). Earlier we investigated the effect of these residues on the rates of refolding and unfolding of the apomyoglobin structure [11]. In this study, we analyze only the influence of single substitutions of hydrophobic amino acid residues on the stability of the molten globule state of apomyoglobin.

Bottom Line: In this study, we have investigated the effect of substitutions of hydrophobic amino acid residues in the hydrophobic core of protein and on its surface on a molten globule type intermediate state of apomyoglobin.It has been found that independent of their localization in protein, substitutions of hydrophobic amino acid residues do not affect the stability of the molten globule state of apomyoglobin.The result obtained allows us not only to conclude which mutations can have an effect on the intermediate state of the molten globule type, but also explains why the introduction of a disulfide bond (which seems to "strengthen" the protein) can result in destabilization of the protein native state of apomyoglobin.

View Article: PubMed Central - PubMed

Affiliation: Institute of Protein Research, RAS, Pushchino, Moscow Region, Russia.

ABSTRACT
At present it is unclear which interactions in proteins reveal the presence of intermediate states, their stability and formation rate. In this study, we have investigated the effect of substitutions of hydrophobic amino acid residues in the hydrophobic core of protein and on its surface on a molten globule type intermediate state of apomyoglobin. It has been found that independent of their localization in protein, substitutions of hydrophobic amino acid residues do not affect the stability of the molten globule state of apomyoglobin. It has been shown also that introduction of a disulfide bond on the protein surface can stabilize the molten globule state. However in the case of apomyoglobin, stabilization of the intermediate state leads to relative destabilization of the native state of apomyoglobin. The result obtained allows us not only to conclude which mutations can have an effect on the intermediate state of the molten globule type, but also explains why the introduction of a disulfide bond (which seems to "strengthen" the protein) can result in destabilization of the protein native state of apomyoglobin.

Show MeSH