ArticleProtein science : a publication of the Protein Society2007
A cross-strand Trp Trp pair stabilizes the hPin1 WW domain at the expense of function.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- An Engineered Solidified Peptide Hemocyte Sponge as Nanomotor Storage to Combat Bacterial Colitis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Tunable CH/π Interactions within a Tryptophan Zipper Motif to Stabilize the Fold of Long β-Hairpin Peptides.ACS chemical biology · 2023Article
- Evaluation of β-Amino Acid Replacements in Protein Loops: Effects on Conformational Stability and Structure.Chembiochem : a European journal of chemical biology · 2018Article
- A pH Switch for β-Sheet Protein Folding.Angewandte Chemie (International ed. in English) · 2017Article
- The Dependence of Carbohydrate-Aromatic Interaction Strengths on the Structure of the Carbohydrate.Journal of the American Chemical Society · 2016Article
- Aryl-aryl interactions in designed peptide folds: Spectroscopic characteristics and optimal placement for structure stabilization.Biopolymers · 2016Article
- The Role of Electrostatic Interactions in Folding of β-Proteins.Journal of the American Chemical Society · 2016Article
- Implications of aromatic-aromatic interactions: From protein structures to peptide models.Protein science : a publication of the Protein Society · 2015Review
- Circular permutation of a WW domain: folding still occurs after excising the turn of the folding-nucleating hairpin.Journal of the American Chemical Society · 2014Article
- Statistical Analysis of Terminal Extensions of Protein β-Strand Pairs.Advances in bioinformatics · 2013Article
- New insights regarding protein folding as learned from beta-sheets.EXCLI journal · 2012Article
- Article
- Redesign of a WW domain peptide for selective recognition of single-stranded DNA.Biochemistry · 2011Article
- Context-dependent effects of asparagine glycosylation on Pin WW folding kinetics and thermodynamics.Journal of the American Chemical Society · 2010Article
- Stabilizing capping motif for beta-hairpins and sheets.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Sequence determinants of thermodynamic stability in a WW domain--an all-beta-sheet protein.Protein science : a publication of the Protein Society · 2009Article
- Article
- Probing the lower size limit for protein-like fold stability: ten-residue microproteins with specific, rigid structures in water.Journal of the American Chemical Society · 2008Article
- Combining experiment and simulation in protein folding: closing the gap for small model systems.Current opinion in structural biology · 2008Review
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4 authors.
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Abstract
Using the human Pin1 WW domain (hPin1 WW), we show that replacement of two nearest neighbor non-hydrogen-bonded residues on adjacent beta-strands with tryptophan (Trp) residues increases beta-sheet thermodynamic stability by 4.8 kJ mol(-1) at physiological temperature. One-dimensional NMR studies confirmed that introduction of the Trp-Trp pair does not globally perturb the structure of the triple-stranded beta-sheet, while circular dichroism studies suggest that the engineered cross-strand Trp-Trp pair adopts a side-chain conformation similar to that first reported for a designed "Trp-zipper" beta-hairpin peptide, wherein the indole side chains stack perpendicular to each other. Even though the mutated side chains in wild-type hPin1 WW are not conserved among WW domains and compose the beta-sheet surface opposite to that responsible for ligand binding, introduction of the cross-strand Trp-Trp pair effectively eliminates hPin1 WW function as assessed by the loss of binding affinity toward a natural peptide ligand. Maximizing both thermodynamic stability and the domain function of hPin1 WW by the above mentioned approach appears to be difficult, analogous to the situation with loop 1 optimization explored previously. That introduction of a non-hydrogen-bonded cross-strand Trp-Trp pair within the hPin1 WW domain eliminates function may provide a rationale for why this energetically favorable pairwise interaction has not yet been identified in WW domains or any other biologically evolved protein with known three-dimensional structure.
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