ArticleBiochemistry2014
WW domain folding complexity revealed by infrared spectroscopy.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed.
- Unveiling hidden intermediate states in protein folding with AI-based conditional transition clustering.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The Role of the Electronic Structure during Protein Folding through Electron Density-Based Quantum Chemical Descriptors.ACS omega · 2026Article
- Discovery and optimization of a synthetic small protein domain targeting antibodies.Frontiers in bioengineering and biotechnology · 2025Article
- Genetically encoded non-canonical amino acids reveal asynchronous dark reversion of chromophore, backbone, and side-chains in EL222.Protein science : a publication of the Protein Society · 2023Article
- Late-Stage Functionalisation of Peptides on the Solid Phase by an Iodination-Substitution Approach.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Simple Model of Protein Energetics To Identify Ab Initio Folding Transitions from All-Atom MD Simulations of Proteins.Journal of chemical theory and computation · 2020Article
- Localizing Frustration in Proteins Using All-Atom Energy Functions.The journal of physical chemistry. B · 2019Article
- A quantitative connection of experimental and simulated folding landscapes by vibrational spectroscopy.Chemical science · 2018Article
- Parallel folding pathways of Fip35 WW domain explained by infrared spectra and their computer simulation.FEBS letters · 2017Article
- Dual time-resolved temperature-jump fluorescence and infrared spectroscopy for the study of fast protein dynamics.Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy · 2017Article
- Submillisecond Dynamics of Mastoparan X Insertion into Lipid Membranes.The journal of physical chemistry letters · 2016Article
- Influence of Glu/Arg, Asp/Arg, and Glu/Lys Salt Bridges on α-Helical Stability and Folding Kinetics.Biophysical journal · 2016Article
- Ligand-Dependent Conformational Dynamics of Dihydrofolate Reductase.Biochemistry · 2016Article
- The Role of Electrostatic Interactions in Folding of β-Proteins.Journal of the American Chemical Society · 2016Article
- EGCG Inhibited Lipofuscin Formation Based on Intercepting Amyloidogenic β-Sheet-Rich Structure Conversion.PloS one · 2016Article
- Preventing fibril formation of a protein by selective mutation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Folding kinetics of WW domains with the united residue force field for bridging microscopic motions and experimental measurements.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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2 authors.
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Abstract
Although the intrinsic tryptophan fluorescence of proteins offers a convenient probe of protein folding, interpretation of the fluorescence spectrum is often difficult because it is sensitive to both global and local changes. Infrared (IR) spectroscopy offers a complementary measure of structural changes involved in protein folding, because it probes changes in the secondary structure of the protein backbone. Here we demonstrate the advantages of using multiple probes, infrared and fluorescence spectroscopy, to study the folding of the FBP28 WW domain. Laser-induced temperature jumps coupled with fluorescence or infrared spectroscopy have been used to probe changes in the peptide backbone on the submillisecond time scale. The relaxation dynamics of the β-sheets and β-turn were measured independently by probing the corresponding IR bands assigned in the amide I region. Using these wavelength-dependent measurements, we observe three kinetics phases, with the fastest process corresponding to the relaxation kinetics of the turns. In contrast, fluorescence measurements of the wild-type WW domain and tryptophan mutants exhibit single-exponential kinetics with a lifetime that corresponds to the slowest phase observed by infrared spectroscopy. Mutant sequences provide evidence of an intermediate dry molten globule state. The slowest step in the folding of this WW domain is the tight packing of the side chains in the transition from the dry molten globule intermediate to the native structure. This study demonstrates that using multiple complementary probes enhances the interpretation of protein folding dynamics.
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