ArticleProtein science : a publication of the Protein Society2002
The role of aromatic residues in the hydrophobic core of the villin headpiece subdomain.
Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Article
- Bst DNA Polymerase: Structure, Properties and Engineering Strategies in LAMP.International journal of molecular sciences · 2026Review
- Co-conserved sequence motifs are predictive of substrate specificity in a family of monotopic phosphoglycosyl transferases.Protein science : a publication of the Protein Society · 2023Article
- Topological data analysis gives two folding paths in HP35(nle-nle), double mutant of villin headpiece subdomain.Scientific reports · 2022Article
- Quantitative Analysis of Protein Unfolded State Energetics: Experimental and Computational Studies Demonstrate That Non-Native Side-Chain Interactions Stabilize Local Native Backbone Structure.The journal of physical chemistry. B · 2021Article
- Deuteration of nonexchangeable protons on proteins affects their thermal stability, side-chain dynamics, and hydrophobicity.Protein science : a publication of the Protein Society · 2020Article
- A conserved and buried edge-to-face aromatic interaction in small ubiquitin-like modifier (SUMO) has a role in SUMO stability and function.The Journal of biological chemistry · 2019Article
- A High-Throughput Mutational Scan of an Intrinsically Disordered Acidic Transcriptional Activation Domain.Cell systems · 2018Article
- The effect of chirality and steric hindrance on intrinsic backbone conformational propensities: tools for protein design.Protein engineering, design & selection : PEDS · 2016Article
- Implications of aromatic-aromatic interactions: From protein structures to peptide models.Protein science : a publication of the Protein Society · 2015Review
- Equilibrium kinetic network of the villin headpiece in implicit solvent.Biophysical journal · 2015Article
- Glassy dynamics of protein methyl groups revealed by deuteron NMR.The journal of physical chemistry. B · 2013Article
- Fast dynamics of HP35 for folded and urea-unfolded conditions.The journal of physical chemistry. B · 2012Article
- Conformational dynamics and stability of HP35 studied with 2D IR vibrational echoes.Journal of the American Chemical Society · 2012Article
- Intrinsic energy landscapes of amino acid side-chains.Journal of chemical information and modeling · 2012Article
- On the unyielding hydrophobic core of villin headpiece.Protein science : a publication of the Protein Society · 2012Article
- Article
- Contribution of hydrophobic interactions to protein stability.Journal of molecular biology · 2011Article
- The CLN025 decapeptide retains a β-hairpin conformation in urea and guanidinium chloride.The journal of physical chemistry. B · 2011Article
- Hydrophobic core formation and dehydration in protein folding studied by generalized-ensemble simulations.Biophysical journal · 2010Article
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4 authors.
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Abstract
Small autonomously folding proteins are of interest as model systems to study protein folding, as the same molecule can be used for both experimental and computational approaches. The question remains as to how well these minimized peptide model systems represent larger native proteins. For example, is the core of a minimized protein tolerant to mutation like larger proteins are? Also, do minimized proteins use special strategies for specifying and stabilizing their folded structure? Here we examine these questions in the 35-residue autonomously folding villin headpiece subdomain (VHP subdomain). Specifically, we focus on a cluster of three conserved phenylalanine (F) residues F47, F51, and F58, that form most of the hydrophobic core. These three residues are oriented such that they may provide stabilizing aromatic-aromatic interactions that could be critical for specifying the fold. Circular dichroism and 1D-NMR spectroscopy show that point mutations that individually replace any of these three residues with leucine were destabilized, but retained the native VHP subdomain fold. In pair-wise replacements, the double mutant that retains F58 can adopt the native fold, while the two double mutants that lack F58 cannot. The folding of the double mutant that retains F58 demonstrates that aromatic-aromatic interactions within the aromatic cluster are not essential for specifying the VHP subdomain fold. The ability of the VHP subdomain to tolerate mutations within its hydrophobic core indicates that the information specifying the three dimensional structure is distributed throughout the sequence, as observed in larger proteins. Thus, the VHP subdomain is a legitimate model for larger, native proteins.
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