Loops linking secondary structure elements affect the stability of the molten globule intermediate state of apomyoglobin

Majorina, Maria A.; Balobanov, Vitaly A.; Uversky, Vladimir N.; Melnik, Bogdan S.

doi:10.1002/1873-3468.13905

Cited by 5 publications

(5 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The protein concentration was 0.2 mg/mL. Changes in the Trp fluorescence spectrum (during heating) were monitored at an intensity of 380 nm (I 380nm ) [ 27 ].…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Oligomerization and Adjuvant Activity of Peptides Derived from the VirB4-like ATPase of Clostridioides difficile

Sorokina,

Sokolova,

Majorina

et al. 2023

Biomolecules

Self Cite

View full text Add to dashboard Cite

In a previous study, we demonstrated that the Clostridioides difficile VirB4-like ATPase forms oligomers in vitro. In the current investigation, to study the observed phenomenon in more detail, we prepared a library of VirB4-derived peptides (delVirB4s) fused to a carrier maltose-binding protein (MBP). Using gel chromatography and polyacrylamide gel electrophoresis, we found a set of overlapping fragments that contribute most significantly to protein aggregation, which were represented as water-soluble oligomers with molecular masses ranging from ~300 kD to several megadaltons. Membrane filtration experiments, sucrose gradient ultracentrifugation, and dynamic light scattering measurements indicated the size of the soluble complex to be 15–100 nm. It was sufficiently stable to withstand treatment with 1 M urea; however, it dissociated in a 6 M urea solution. As shown by the changes in GFP fluorescence and the circular dichroism spectra, the attachment of the delVirB4 peptide significantly altered the structure of the partner MBP. The immunization of mice with the hybrid consisting of the selected VirB4-derived peptide and MBP, GST, or GFP resulted in increased production of specific antibodies compared to the peptide-free carrier proteins, suggesting significant adjuvant activity of the VirB4 fragment. This feature could be useful for the development of new vaccines, especially in the case of “weak” antigens that are unable to elicit a strong immune response by themselves.

show abstract

“…The protein concentration was 0.2 mg/mL. Changes in the Trp fluorescence spectrum (during heating) were monitored at an intensity of 380 nm (I 380nm ) [ 27 ].…”

Section: Methodsmentioning

confidence: 99%

“…Light scattering was measured at an angle of 173 degrees. The data were analyzed using Malvern software (https://www.malvernpanalytical.com, accessed on 15 June 2023) [27].…”

Section: Biophysical Methodsmentioning

confidence: 99%

Oligomerization and Adjuvant Activity of Peptides Derived from the VirB4-like ATPase of Clostridioides difficile

Sorokina,

Sokolova,

Majorina

et al. 2023

Biomolecules

Self Cite

View full text Add to dashboard Cite

show abstract

“…63,66,85,86 Loop regions, denatured proteins and even some peptides have been shown to not be completely disordered. [87][88][89][90][91][92][93][94][95][96][97][98][99][100][101][102] In the light of the above, in Table 1 we summarize the works that have been carried out with the aim of calibrating RCCSs. One can observe that database-derived, statistical approaches have recently been gaining popularity.…”

Section: Determining Rccss: An Ill-defined Calibration Problemmentioning

confidence: 99%

“…63,66,85,86 Loop regions, denatured proteins and even some peptides have been shown to not be completely disordered. 87–102…”

Section: Determining Rccss: An Ill-defined Calibration Problemmentioning

confidence: 99%

The influence of random-coil chemical shifts on the assessment of structural propensities in folded proteins and IDPs

Kovács

Bodor

2023

RSC Adv.

View full text Add to dashboard Cite

show abstract

“…Elongation/shortening of loops on the protein surface destabilizes the state of the molten globule type relative to the unfolded state of the protein Majorina et al, (2020).…”

Section: Schematic Representation Of a Protein And Substitutionsmentioning

confidence: 99%

Some useful ideas for multistate protein design: Effect of amino acid substitutions on the multistate proteins stability and the rate of protein structure formation

Majorina

Melnik

Glukhov

et al. 2022

Front. Mol. Biosci.

View full text Add to dashboard Cite

The design of new protein variants is usually confined to slightly “fixing” an already existing protein, adapting it to certain conditions or to a new substrate. This is relatively easy to do if the fragment of the protein to be affected, such as the active site of the protein, is known. But what if you need to “fix” the stability of a protein or the rate of its native or intermediate state formation? Having studied a large number of protein mutant forms, we have established the effect of various amino acid substitutions on the energy landscape of the protein. As a result, we have revealed a number of patterns to help researchers identify amino acid residues that determine the folding rate and the stability of globular proteins states and design a mutant form of a protein with desired properties.

show abstract

Loops linking secondary structure elements affect the stability of the molten globule intermediate state of apomyoglobin

Cited by 5 publications

References 32 publications

Oligomerization and Adjuvant Activity of Peptides Derived from the VirB4-like ATPase of Clostridioides difficile

Oligomerization and Adjuvant Activity of Peptides Derived from the VirB4-like ATPase of Clostridioides difficile

The influence of random-coil chemical shifts on the assessment of structural propensities in folded proteins and IDPs

Some useful ideas for multistate protein design: Effect of amino acid substitutions on the multistate proteins stability and the rate of protein structure formation

Contact Info

Product

Resources

About