ArticleBiophysical journal2014
Rigidity, secondary structure, and the universality of the boson peak in proteins.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed.
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- Effect of a Self-Assembly Peptide on Surface Roughness and Hardness of Bleached Enamel.Journal of functional biomaterials · 2022Article
- Analysis of the Factors Affecting Static In Vitro Pepsinolysis of Food Proteins.Molecules (Basel, Switzerland) · 2022Article
- Controlling the Substrate Specificity of an Enzyme through Structural Flexibility by Varying the Salt-Bridge Density.Molecules (Basel, Switzerland) · 2021Article
- Local Electric Field Controls Fluorescence Quantum Yield of Red and Far-Red Fluorescent Proteins.Frontiers in molecular biosciences · 2021Article
- Intrinsically disordered proteins access a range of hysteretic phase separation behaviors.Science advances · 2019Article
- Universality and Structural Implications of the Boson Peak in Proteins.Biophysical journal · 2019Article
- Redox chemistry in the pigment eumelanin as a function of temperature using broadband dielectric spectroscopy.RSC advances · 2019Article
- Boson peak, heterogeneity and intermediate-range order in binary SiOScientific reports · 2018Article
- Olefin metathesis catalysts embedded in β-barrel proteins: creating artificial metalloproteins for olefin metathesis.Beilstein journal of organic chemistry · 2018Review
- Identification of coding sequence and its use for functional and structural characterization of catalase fromBioinformation · 2018Article
- Observation of dielectric universalities in albumin, cytochrome C and Shewanella oneidensis MR-1 extracellular matrix.Scientific reports · 2017Article
- Viscoelasticity of amyloid plaques in transgenic mouse brain studied by Brillouin microspectroscopy and correlative Raman analysis.Journal of innovative optical health sciences · 2017Article
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4 authors.
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Abstract
Complementary neutron- and light-scattering results on nine proteins and amino acids reveal the role of rigidity and secondary structure in determining the time- and lengthscales of low-frequency collective vibrational dynamics in proteins. These dynamics manifest in a spectral feature, known as the boson peak (BP), which is common to all disordered materials. We demonstrate that BP position scales systematically with structural motifs, reflecting local rigidity: disordered proteins appear softer than α-helical proteins; which are softer than β-sheet proteins. Our analysis also reveals a universal spectral shape of the BP in proteins and amino acid mixtures; superimposable on the shape observed in typical glasses. Uniformity in the underlying physical mechanism, independent of the specific chemical composition, connects the BP vibrations to nanometer-scale heterogeneities, providing an experimental benchmark for coarse-grained simulations, structure/rigidity relationships, and engineering of proteins for novel applications.
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