Hydrophobic sequence minimization of the -lactalbumin molten globule
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 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 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 کاملSugar-induced molten-globule model.
Proteins denature at low pH because of intramolecular electrostatic repulsions. The addition of salt partially overcomes this repulsion for some proteins, yielding a collapsed conformation called the A-state. A-states have characteristics expected for the molten globule, a notional kinetic protein folding intermediate. Here we show that the addition of neutral sugars to solutions of acid-denatu...
متن کاملDifferent subdomains are most protected from hydrogen exchange in the molten globule and native states of human alpha-lactalbumin.
alpha-Lactalbumin (alpha-LA) is a two-domain, calcium-binding protein that forms one of the best studied molten globules. We present here amide hydrogen exchange studies of the molten globule formed by human alpha-LA at pH 2 and compare these results with a similar study of the native state at pH 6.3. The most persistent structure in the molten globule is localized in the helical domain, consis...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1997
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.94.26.14314