FEBS letters, 2017-10, Vol.591 (20), p.3265-3275
2017
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Details
- Autor(en) / Beteiligte
- Titel
- Parallel folding pathways of Fip35 WW domain explained by infrared spectra and their computer simulation
- Ist Teil von
- FEBS letters, 2017-10, Vol.591 (20), p.3265-3275
- Ort / Verlag
- England
- Erscheinungsjahr
- 2017
- Quelle
- Free E-Journal (出版社公開部分のみ）
- Beschreibungen/Notizen
- We present a calculation of the amide I′ infrared (IR) spectra of the folded, unfolded, and intermediate states of the WW domain Fip35, a model system for β‐sheet folding. Using an all‐atom molecular dynamics simulation in which multiple folding and unfolding events take place we identify six conformational states and then apply perturbed matrix method quantum‐mechanical calculations to determine their amide I′ IR spectra. Our analysis focuses on two states previously identified as Fip35 folding intermediates and suggests that a three‐stranded core similar to the folded state core is the main source of the spectroscopic differences between the two intermediates. In particular, we propose a hypothesis for why folding via one of these intermediates was not experimentally observed by IR T‐jump.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0014-5793eISSN: 1873-3468DOI: 10.1002/1873-3468.12836Titel-ID: cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5658256
- Format
- –
- Schlagworte
- Amino Acid Motifs, fast‐folding peptides, Kinetics, Models, Molecular, Molecular Dynamics Simulation, molecular dynamics simulations, NIMA-Interacting Peptidylprolyl Isomerase - chemistry, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Domains, Protein Engineering, Protein Folding, Protein Unfolding, Quantum Theory, Spectrophotometry, Infrared, Thermodynamics, β‐hairpin