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.

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Melnik, T. A., Majorina, M. A., Larina, D. S., Kashparov, I. A., Samatova, E. N., Glukhov, A. S., et al. (2014). 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. PLoS One, 9(6): e98645. doi:10.1371/journal.pone.0098645.

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Basic (Discarded)

Date of Discard: 2015-06-02

Comment:

Creators:
Melnik, T. A.
Majorina, M. A.
Larina, D. S.
Kashparov, I. A.
Samatova, E. N.¹
Glukhov, A. S.
Melnik, B. S.

Affiliations:
1Department of Physical Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_578598

Dates: Published Online: 2014-06-03

Files: 1 File

Locators: 1 Locator

version ID: item_2042824_3

Item State: Discarded

Name of Context: Publications of the MPI for Biophysical Chemistry, Affiliated to: MPI for Biophysical Chemistry