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Residue solvent accessibilities in the unfolded polypeptide chain.

The difference of solvent accessibilities in the native and unfolded states of the protein is used as a measure of the hydrophobic contribution to the free energy of folding. We present a new approximation of amino acids solvent accessibilities in the unfolded state based on the 1-ns molecular dynam...

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Detaylı Bibliyografya
Asıl Yazarlar: Zielenkiewicz, P, Saenger, W
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: 1992
Konular:
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC1262262/
https://ncbi.nlm.nih.gov/pubmed/1489908
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