Nascent β-Hairpin Formation of a Natively Unfolded Peptide Reveals the Role of Hydrophobic Contacts

Despite the important role of the unfolded states in protein stability, folding, and aggregation, they remain poorly understood due to the lack of residue-specific experimental data. Here, we explore features of the unfolded state of the NTL9 protein by applying all-atom replica-exchange simulations...

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Veröffentlicht in:	Biophysical journal 2015-08, Vol.109 (3), p.630-638
Hauptverfasser:	Chen, Wei, Shi, Chuanyin, Shen, Jana
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Motifs Amino Acid Sequence Hydrogen Bonding Hydrophobic and Hydrophilic Interactions Molecular Dynamics Simulation Molecular Sequence Data Peptides - chemistry Protein Structure, Tertiary Protein Unfolding Proteins and Nucleic Acids Ribosomal Proteins - chemistry Static Electricity
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