Increased exposure of hydrophobic surface in molten globule state of alpha-lactalbumin. Fluorescence and hydrophobic photolabeling studies.
نویسندگان
چکیده
منابع مشابه
Hydrophobic sequence minimization of the alpha-lactalbumin molten globule.
The molten globule, a widespread protein-folding intermediate, can attain a native-like backbone topology, even in the apparent absence of rigid side-chain packing. Nonetheless, mutagenesis studies suggest that molten globules are stabilized by some degree of side-chain packing among specific hydrophobic residues. Here we investigate the importance of hydrophobic side-chain diversity in determi...
متن کاملEntropy calculations on the molten globule state of a protein: side-chain entropies of alpha-lactalbumin.
We present entropy estimates based on molecular dynamics simulations of models of the molten globule state of the protein alpha-lactalbumin at low pH. The entropy calculations use the covariance matrix of atom-positional fluctuations and yield the complete configurational entropy. The configurational entropy of the entire protein and of each of its side chains is calculated. Exposed side chains...
متن کامل1,1,1,3,3,3-hexafluoroisopropanol induced thermal unfolding and molten globule state of bovine alpha-lactalbumin: calorimetric and spectroscopic studies.
The thermal denaturation of alpha-lactalbumin was studied at pH 7.0 and 9.0 in aqueous 1,1,1,3,3,3-hexafluoroisopropanol (HFIP) by high-sensitivity differential scanning calorimetry. The conformation of the protein was analyzed by a combination of fluorescence and circular dichroism measurements. The most obvious effect of HFIP was lowering of the transition temperature with an increase in the ...
متن کاملDefining the core structure of the alpha-lactalbumin molten globule state.
Molten globules are partially folded states of proteins which are generally believed to mimic structures formed during the folding process. In order to determine the minimal requirements for the formation of a molten globule state, we have prepared a set of peptide models of the molten globule state of human alpha-lactalbumin (alphaLA). A peptide consisting of residues 1-38 crosslinked, via the...
متن کاملOrganization and dynamics of tryptophans in the molten globule state of bovine alpha-lactalbumin utilizing wavelength-selective fluorescence approach: comparisons with native and denatured states.
Bovine alpha-lactalbumin (BLA) is known to be present in molten globule form in its apo-state (i.e., Ca(2+) depleted state). We explored the organization and dynamics of the functionally important tryptophan residues of BLA in native, molten globule and denatured states utilizing the wavelength-selective fluorescence approach. We observed red edge excitation shift (REES) of 7 nm for the tryptop...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1992
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)88643-x