The Experts below are selected from a list of 306 Experts worldwide ranked by ideXlab platform
Hiroshi Takano - One of the best experts on this subject based on the ideXlab platform.
-
folding pathways of nug2 a designed mutant of protein g using Relaxation Mode analysis
Journal of Chemical Physics, 2019Co-Authors: Ayori Mitsutake, Hiroshi TakanoAbstract:Dynamic analysis methods are important for analyzing long simulations such as folding simulations. Relaxation Mode analysis, which approximately extracts slow Modes and rates, has been applied in molecular dynamics (MD) simulations of protein systems. Previously, we showed that slow Modes are suitable for analyzing simulations in which large conformational changes occur. Here, we applied Relaxation Mode analysis to folding simulations of a designed mutant of protein G, NuG2, to investigate its folding pathways. The folding simulations of NuG2 were previously performed for this mutant with Anton. In the present study, the free energy surfaces were calculated by projecting the coordinates on the axis of the slow Relaxation Modes obtained from Relaxation Mode analysis. We classified various characteristic states such as native, nativelike, intermediate, and random states and clarified two main folding pathways. In the early folding process, the first and second β strands formed an N-terminal β-sheet. After the early folding process, the fourth β strand formed along the first β strand in the same or opposite direction as the native structure; two characteristic intermediate states were identified. Finally, the intermediate structures folded to the native structure in the folding process. Relaxation Mode analysis can be applied to folding simulations of complex proteins to investigate their folding processes.Dynamic analysis methods are important for analyzing long simulations such as folding simulations. Relaxation Mode analysis, which approximately extracts slow Modes and rates, has been applied in molecular dynamics (MD) simulations of protein systems. Previously, we showed that slow Modes are suitable for analyzing simulations in which large conformational changes occur. Here, we applied Relaxation Mode analysis to folding simulations of a designed mutant of protein G, NuG2, to investigate its folding pathways. The folding simulations of NuG2 were previously performed for this mutant with Anton. In the present study, the free energy surfaces were calculated by projecting the coordinates on the axis of the slow Relaxation Modes obtained from Relaxation Mode analysis. We classified various characteristic states such as native, nativelike, intermediate, and random states and clarified two main folding pathways. In the early folding process, the first and second β strands formed an N-terminal β-sheet. After t...
-
Folding pathways of NuG2—a designed mutant of protein G—using Relaxation Mode analysis
Journal of Chemical Physics, 2019Co-Authors: Ayori Mitsutake, Hiroshi TakanoAbstract:Dynamic analysis methods are important for analyzing long simulations such as folding simulations. Relaxation Mode analysis, which approximately extracts slow Modes and rates, has been applied in molecular dynamics (MD) simulations of protein systems. Previously, we showed that slow Modes are suitable for analyzing simulations in which large conformational changes occur. Here, we applied Relaxation Mode analysis to folding simulations of a designed mutant of protein G, NuG2, to investigate its folding pathways. The folding simulations of NuG2 were previously performed for this mutant with Anton. In the present study, the free energy surfaces were calculated by projecting the coordinates on the axis of the slow Relaxation Modes obtained from Relaxation Mode analysis. We classified various characteristic states such as native, nativelike, intermediate, and random states and clarified two main folding pathways. In the early folding process, the first and second β strands formed an N-terminal β-sheet. After the early folding process, the fourth β strand formed along the first β strand in the same or opposite direction as the native structure; two characteristic intermediate states were identified. Finally, the intermediate structures folded to the native structure in the folding process. Relaxation Mode analysis can be applied to folding simulations of complex proteins to investigate their folding processes.Dynamic analysis methods are important for analyzing long simulations such as folding simulations. Relaxation Mode analysis, which approximately extracts slow Modes and rates, has been applied in molecular dynamics (MD) simulations of protein systems. Previously, we showed that slow Modes are suitable for analyzing simulations in which large conformational changes occur. Here, we applied Relaxation Mode analysis to folding simulations of a designed mutant of protein G, NuG2, to investigate its folding pathways. The folding simulations of NuG2 were previously performed for this mutant with Anton. In the present study, the free energy surfaces were calculated by projecting the coordinates on the axis of the slow Relaxation Modes obtained from Relaxation Mode analysis. We classified various characteristic states such as native, nativelike, intermediate, and random states and clarified two main folding pathways. In the early folding process, the first and second β strands formed an N-terminal β-sheet. After t...
-
Identification of slow Relaxation Modes in a protein trimer via positive definite Relaxation Mode analysis.
Journal of Chemical Physics, 2019Co-Authors: Naoyuki Karasawa, Ayori Mitsutake, Hiroshi TakanoAbstract:Recently, dynamic analysis methods in signal processing have been applied to the analysis of molecular dynamics (MD) trajectories of biopolymers. In the context of a Relaxation Mode analysis (RMA) method, based on statistical physics, it is explained why the signal-processing methods work well for the simulation trajectories of biopolymers. A distinctive difference between the RMA method and the signal-processing methods is the introduction of an additional parameter, called an evolution time parameter. This parameter enables us to better estimate the Relaxation Modes and rates, although it increases computational difficulty. In this paper, we propose a simple and effective extension of the RMA method, which is referred to as the positive definite RMA method, to introduce the evolution time parameter robustly. In this method, an eigenvalue problem for the time correlation matrix of physical quantities relevant to slow Relaxation in a system is first solved to find the subspace in which the matrix is numerically positive definite. Then, we implement the RMA method in the subspace. We apply the method to the analysis of a 3-μs MD trajectory of a heterotrimer of an erythropoietin protein and two of its receptor proteins, and we demonstrate the effectiveness of the method.Recently, dynamic analysis methods in signal processing have been applied to the analysis of molecular dynamics (MD) trajectories of biopolymers. In the context of a Relaxation Mode analysis (RMA) method, based on statistical physics, it is explained why the signal-processing methods work well for the simulation trajectories of biopolymers. A distinctive difference between the RMA method and the signal-processing methods is the introduction of an additional parameter, called an evolution time parameter. This parameter enables us to better estimate the Relaxation Modes and rates, although it increases computational difficulty. In this paper, we propose a simple and effective extension of the RMA method, which is referred to as the positive definite RMA method, to introduce the evolution time parameter robustly. In this method, an eigenvalue problem for the time correlation matrix of physical quantities relevant to slow Relaxation in a system is first solved to find the subspace in which the matrix is numer...
-
identification of slow Relaxation Modes in a protein trimer via positive definite Relaxation Mode analysis
Journal of Chemical Physics, 2019Co-Authors: Naoyuki Karasawa, Ayori Mitsutake, Hiroshi TakanoAbstract:: Recently, dynamic analysis methods in signal processing have been applied to the analysis of molecular dynamics (MD) trajectories of biopolymers. In the context of a Relaxation Mode analysis (RMA) method, based on statistical physics, it is explained why the signal-processing methods work well for the simulation trajectories of biopolymers. A distinctive difference between the RMA method and the signal-processing methods is the introduction of an additional parameter, called an evolution time parameter. This parameter enables us to better estimate the Relaxation Modes and rates, although it increases computational difficulty. In this paper, we propose a simple and effective extension of the RMA method, which is referred to as the positive definite RMA method, to introduce the evolution time parameter robustly. In this method, an eigenvalue problem for the time correlation matrix of physical quantities relevant to slow Relaxation in a system is first solved to find the subspace in which the matrix is numerically positive definite. Then, we implement the RMA method in the subspace. We apply the method to the analysis of a 3-μs MD trajectory of a heterotrimer of an erythropoietin protein and two of its receptor proteins, and we demonstrate the effectiveness of the method.
-
Relaxation Mode analysis for molecular dynamics simulations of proteins.
Biophysical Reviews, 2018Co-Authors: Ayori Mitsutake, Hiroshi TakanoAbstract:Molecular dynamics simulation is a powerful method for investigating the structural stability, dynamics, and function of biopolymers at the atomic level. In recent years, it has become possible to perform simulations on time scales of the order of milliseconds using special hardware. However, it is necessary to derive the important factors contributing to structural change or function from the complicated movements of biopolymers obtained from long simulations. Although some analysis methods for protein systems have been developed using increasing simulation times, many of these methods are static in nature (i.e., no information on time). In recent years, dynamic analysis methods have been developed, such as the Markov state Model and Relaxation Mode analysis (RMA), which was introduced based on spin and homopolymer systems. The RMA method approximately extracts slow Relaxation Modes and rates from trajectories and decomposes the structural fluctuations into slow Relaxation Modes, which characterize the slow Relaxation dynamics of the system. Recently, this method has been applied to biomolecular systems. In this article, we review RMA and its improved versions for protein systems.
Colette Lacabanne - One of the best experts on this subject based on the ideXlab platform.
-
Thermal ageing of PTFE in the melted state: Influence of interdiffusion on the physicochemical structure
Polymer Degradation and Stability, 2020Co-Authors: Victor Henri, Colette Lacabanne, Eric Dantras, Anca Goleanu Dieudonne, Flavien KoliateneAbstract:PTFE is one of the most used polymer for electrical insulation. For future aircraft, PTFE will be exposed to thermal constraints above its melting temperature. Its high melt viscosity allows PTFE to be operable but it will be subjected to thermal-oxidative ageing. PTFE presents two initial states, associated with its thermal history corresponding to the interdiffusion phenomenon. In the case of thermo-oxidative ageing in the melt, interdiffusion impairs the thermal stability by shifting the thermal degradation towards lower temperature. While interdiffusion reduces the thermal stability for long time ageing, strong physical interactions reduce the impact of degradation on the mechanical behaviour for short time ageing. Chemical ageing induced by degradation promotes recrystallisation of PTFE shorter chains; this crystalline phase modifies the β anelastic Relaxation Mode. The tan δ thermograms allows us to identify the β1 and β2 components of the anelastic effects of respectively the triclinic/hexagonal and hexagonal/pseudo hexagonal transitions observed by X-Rays Diffraction. Upon chemical ageing, the evolution of the β Mode is mainly governed by the decrease in the β2 component corresponding to the pseudo-hexagonal phase.
-
Dielectric study of dendritic macromolecules
2000 Eighth International Conference on Dielectric Materials Measurements and Applications (IEE Conf. Publ. No. 473), 2000Co-Authors: E. Dantras, A.m. Caminade, J.p. Majoral, Colette LacabanneAbstract:Combined D.D.S. and T.S.C, techniques allow us to follow temperature and frequency dependence of Relaxation Mode, and gives us more information about behaviour law and molecular mobility of dendrimers. Dipolar nature of the Relaxation Modes in those phosphorus-containing dendrimers has been shown. Evolution from a simple Relaxation Mode (G'/sub 0/) to a complex Relaxation Mode (G'/sub 2/), comes into sight as an influence of specific architecture. Global polarisation increases with generation by discrete additional dipolar Relaxation. Generation looks to be directly linked with the dielectric polarisation of those macromolecules.
-
Physical aging and tacticity effects on the α Relaxation Mode of amorphous polymers by thermally stimulated techniques
Journal of Non-crystalline Solids, 1998Co-Authors: S. Doulut, A. Bernes, C. Bacharan, P. Demont, Colette LacabanneAbstract:Abstract Samples of amorphous poly (ethylene terephthalate) (PET) vitrified under different cooling rates and a series of samples of poly (methyl methacrylate) (PMMA) of various tacticities have been characterized by differential scanning calorimetry (DSC), thermally stimulated current (TSC) and thermally stimulated creep (TSCr). The α Relaxation and retardation Modes, associated with the glass transition, have been analyzed. The dielectric Relaxation Mode observed in PET has Relaxation times following a compensation law with compensation parameters independent of physical aging. Contrarily, the maximum value of the activation enthalpy increases upon aging. The anelastic retardation Mode observed in PMMA is also constituted of retardation times following a compensation law. In that case, the T c − T g lag varies according to the chain conformation. It is also interesting to note that the maximum of the activation enthalpy increases with the level of local interactions. This evolution is due to the increasing of the domain sizes in which molecular mobility takes place.
-
Thermally stimulated current characterization of poly(ether ether ketone) (PEEK)
Conference Record of the 1992 IEEE International Symposium on Electrical Insulation, 1992Co-Authors: M. Mourgues-martin, A. Bernes, Colette LacabanneAbstract:Thermally stimulated current (TSC) spectroscopy was applied to the characterization of poly(ether ether ketone) (PEEK). The dielectric Relaxation Mode associated with the glass transition was analyzed as a function of the degree of crystallinity. The aim was to characterize the microstructure of the amorphous phase. The effect of the degree of crystallinity on the coupling of the crystalline and the amorphous phase was investigated. The authors used differential scanning calorimetry (DSC) as a reference technique for determination of the transition spectra. Thermograms were recorded at a scanning rate of 20 K/min/sup -1/. PEEK was supplied in the form of sheets with a thickness of 0.25 mm; the degree of crystallinity was 10%. A compensation study with sheets having 28% degree of crystallinity was carried out. The dielectric Relaxation Mode association with the glass transition showed the existence of two amorphous phases.
-
Thermally stimulated current characterization of poly(ether ether\nketone) [PEEK]
Conference Record of the 1992 IEEE International Symposium on Electrical Insulation, 1992Co-Authors: M. Mourgues-martin, A. Bernes, Colette LacabanneAbstract:Thermally stimulated current (TSC) spectroscopy was applied to the\ncharacterization of poly(ether ether ketone) [PEEK]. The dielectric\nRelaxation Mode associated with the glass transition was analyzed as a\nfunction of the degree of crystallinity. The aim was to characterize the\nmicrostructure of the amorphous phase. The effect of the degree of\ncrystallinity on the coupling of the crystalline and the amorphous phase\nwas investigated. The authors used differential scanning calorimetry\n(DSC) as a reference technique for determination of the transition\nspectra. Thermograms were recorded at a scanning rate of 20 K/min-1\n. PEEK was supplied in the form of sheets with a thickness of 0.25\nmm; the degree of crystallinity was 10%. A compensation study with\nsheets having 28% degree of crystallinity was carried out. The\ndielectric Relaxation Mode association with the glass transition showed\nthe existence of two amorphous phases
Ayori Mitsutake - One of the best experts on this subject based on the ideXlab platform.
-
folding pathways of nug2 a designed mutant of protein g using Relaxation Mode analysis
Journal of Chemical Physics, 2019Co-Authors: Ayori Mitsutake, Hiroshi TakanoAbstract:Dynamic analysis methods are important for analyzing long simulations such as folding simulations. Relaxation Mode analysis, which approximately extracts slow Modes and rates, has been applied in molecular dynamics (MD) simulations of protein systems. Previously, we showed that slow Modes are suitable for analyzing simulations in which large conformational changes occur. Here, we applied Relaxation Mode analysis to folding simulations of a designed mutant of protein G, NuG2, to investigate its folding pathways. The folding simulations of NuG2 were previously performed for this mutant with Anton. In the present study, the free energy surfaces were calculated by projecting the coordinates on the axis of the slow Relaxation Modes obtained from Relaxation Mode analysis. We classified various characteristic states such as native, nativelike, intermediate, and random states and clarified two main folding pathways. In the early folding process, the first and second β strands formed an N-terminal β-sheet. After the early folding process, the fourth β strand formed along the first β strand in the same or opposite direction as the native structure; two characteristic intermediate states were identified. Finally, the intermediate structures folded to the native structure in the folding process. Relaxation Mode analysis can be applied to folding simulations of complex proteins to investigate their folding processes.Dynamic analysis methods are important for analyzing long simulations such as folding simulations. Relaxation Mode analysis, which approximately extracts slow Modes and rates, has been applied in molecular dynamics (MD) simulations of protein systems. Previously, we showed that slow Modes are suitable for analyzing simulations in which large conformational changes occur. Here, we applied Relaxation Mode analysis to folding simulations of a designed mutant of protein G, NuG2, to investigate its folding pathways. The folding simulations of NuG2 were previously performed for this mutant with Anton. In the present study, the free energy surfaces were calculated by projecting the coordinates on the axis of the slow Relaxation Modes obtained from Relaxation Mode analysis. We classified various characteristic states such as native, nativelike, intermediate, and random states and clarified two main folding pathways. In the early folding process, the first and second β strands formed an N-terminal β-sheet. After t...
-
Folding pathways of NuG2—a designed mutant of protein G—using Relaxation Mode analysis
Journal of Chemical Physics, 2019Co-Authors: Ayori Mitsutake, Hiroshi TakanoAbstract:Dynamic analysis methods are important for analyzing long simulations such as folding simulations. Relaxation Mode analysis, which approximately extracts slow Modes and rates, has been applied in molecular dynamics (MD) simulations of protein systems. Previously, we showed that slow Modes are suitable for analyzing simulations in which large conformational changes occur. Here, we applied Relaxation Mode analysis to folding simulations of a designed mutant of protein G, NuG2, to investigate its folding pathways. The folding simulations of NuG2 were previously performed for this mutant with Anton. In the present study, the free energy surfaces were calculated by projecting the coordinates on the axis of the slow Relaxation Modes obtained from Relaxation Mode analysis. We classified various characteristic states such as native, nativelike, intermediate, and random states and clarified two main folding pathways. In the early folding process, the first and second β strands formed an N-terminal β-sheet. After the early folding process, the fourth β strand formed along the first β strand in the same or opposite direction as the native structure; two characteristic intermediate states were identified. Finally, the intermediate structures folded to the native structure in the folding process. Relaxation Mode analysis can be applied to folding simulations of complex proteins to investigate their folding processes.Dynamic analysis methods are important for analyzing long simulations such as folding simulations. Relaxation Mode analysis, which approximately extracts slow Modes and rates, has been applied in molecular dynamics (MD) simulations of protein systems. Previously, we showed that slow Modes are suitable for analyzing simulations in which large conformational changes occur. Here, we applied Relaxation Mode analysis to folding simulations of a designed mutant of protein G, NuG2, to investigate its folding pathways. The folding simulations of NuG2 were previously performed for this mutant with Anton. In the present study, the free energy surfaces were calculated by projecting the coordinates on the axis of the slow Relaxation Modes obtained from Relaxation Mode analysis. We classified various characteristic states such as native, nativelike, intermediate, and random states and clarified two main folding pathways. In the early folding process, the first and second β strands formed an N-terminal β-sheet. After t...
-
Identification of slow Relaxation Modes in a protein trimer via positive definite Relaxation Mode analysis.
Journal of Chemical Physics, 2019Co-Authors: Naoyuki Karasawa, Ayori Mitsutake, Hiroshi TakanoAbstract:Recently, dynamic analysis methods in signal processing have been applied to the analysis of molecular dynamics (MD) trajectories of biopolymers. In the context of a Relaxation Mode analysis (RMA) method, based on statistical physics, it is explained why the signal-processing methods work well for the simulation trajectories of biopolymers. A distinctive difference between the RMA method and the signal-processing methods is the introduction of an additional parameter, called an evolution time parameter. This parameter enables us to better estimate the Relaxation Modes and rates, although it increases computational difficulty. In this paper, we propose a simple and effective extension of the RMA method, which is referred to as the positive definite RMA method, to introduce the evolution time parameter robustly. In this method, an eigenvalue problem for the time correlation matrix of physical quantities relevant to slow Relaxation in a system is first solved to find the subspace in which the matrix is numerically positive definite. Then, we implement the RMA method in the subspace. We apply the method to the analysis of a 3-μs MD trajectory of a heterotrimer of an erythropoietin protein and two of its receptor proteins, and we demonstrate the effectiveness of the method.Recently, dynamic analysis methods in signal processing have been applied to the analysis of molecular dynamics (MD) trajectories of biopolymers. In the context of a Relaxation Mode analysis (RMA) method, based on statistical physics, it is explained why the signal-processing methods work well for the simulation trajectories of biopolymers. A distinctive difference between the RMA method and the signal-processing methods is the introduction of an additional parameter, called an evolution time parameter. This parameter enables us to better estimate the Relaxation Modes and rates, although it increases computational difficulty. In this paper, we propose a simple and effective extension of the RMA method, which is referred to as the positive definite RMA method, to introduce the evolution time parameter robustly. In this method, an eigenvalue problem for the time correlation matrix of physical quantities relevant to slow Relaxation in a system is first solved to find the subspace in which the matrix is numer...
-
identification of slow Relaxation Modes in a protein trimer via positive definite Relaxation Mode analysis
Journal of Chemical Physics, 2019Co-Authors: Naoyuki Karasawa, Ayori Mitsutake, Hiroshi TakanoAbstract:: Recently, dynamic analysis methods in signal processing have been applied to the analysis of molecular dynamics (MD) trajectories of biopolymers. In the context of a Relaxation Mode analysis (RMA) method, based on statistical physics, it is explained why the signal-processing methods work well for the simulation trajectories of biopolymers. A distinctive difference between the RMA method and the signal-processing methods is the introduction of an additional parameter, called an evolution time parameter. This parameter enables us to better estimate the Relaxation Modes and rates, although it increases computational difficulty. In this paper, we propose a simple and effective extension of the RMA method, which is referred to as the positive definite RMA method, to introduce the evolution time parameter robustly. In this method, an eigenvalue problem for the time correlation matrix of physical quantities relevant to slow Relaxation in a system is first solved to find the subspace in which the matrix is numerically positive definite. Then, we implement the RMA method in the subspace. We apply the method to the analysis of a 3-μs MD trajectory of a heterotrimer of an erythropoietin protein and two of its receptor proteins, and we demonstrate the effectiveness of the method.
-
Relaxation Mode analysis for molecular dynamics simulations of proteins.
Biophysical Reviews, 2018Co-Authors: Ayori Mitsutake, Hiroshi TakanoAbstract:Molecular dynamics simulation is a powerful method for investigating the structural stability, dynamics, and function of biopolymers at the atomic level. In recent years, it has become possible to perform simulations on time scales of the order of milliseconds using special hardware. However, it is necessary to derive the important factors contributing to structural change or function from the complicated movements of biopolymers obtained from long simulations. Although some analysis methods for protein systems have been developed using increasing simulation times, many of these methods are static in nature (i.e., no information on time). In recent years, dynamic analysis methods have been developed, such as the Markov state Model and Relaxation Mode analysis (RMA), which was introduced based on spin and homopolymer systems. The RMA method approximately extracts slow Relaxation Modes and rates from trajectories and decomposes the structural fluctuations into slow Relaxation Modes, which characterize the slow Relaxation dynamics of the system. Recently, this method has been applied to biomolecular systems. In this article, we review RMA and its improved versions for protein systems.
B Roessli - One of the best experts on this subject based on the ideXlab platform.
-
disorder and Relaxation Mode in the lattice dynamics of thepbmg1 3nb2 3o3relaxor ferroelectric
Physical Review B, 2004Co-Authors: S. N. Gvasaliya, S. G. Lushnikov, B RoessliAbstract:The low-energy part of vibration spectrum in PbMg 1 / 3 Nb 2 / 3 O 3 (PMN) relaxor ferroelectric was studied by inelastic neutron scattering. We observed the coexistence of a resolution-limited central peak with strong quasielastic scattering. The line width of the quasielastic component follows a Γ 0 +Dq 1 dependence. We find that Γ 0 is temperature dependent. The Relaxation time follows the Arrhenius law well. The presence of a Relaxation Mode associated with quasielastic scattering in PMN indicates that order-disorder behavior plays an important role in the dynamics of diffuse phase transitions.
-
Disorder and Relaxation Mode in the lattice dynamics of thePbMg1/3Nb2/3O3relaxor ferroelectric
Physical Review B, 2004Co-Authors: Severian Gvasaliya, S. G. Lushnikov, B RoessliAbstract:The low-energy part of vibration spectrum in PbMg 1 / 3 Nb 2 / 3 O 3 (PMN) relaxor ferroelectric was studied by inelastic neutron scattering. We observed the coexistence of a resolution-limited central peak with strong quasielastic scattering. The line width of the quasielastic component follows a Γ 0 +Dq 1 dependence. We find that Γ 0 is temperature dependent. The Relaxation time follows the Arrhenius law well. The presence of a Relaxation Mode associated with quasielastic scattering in PMN indicates that order-disorder behavior plays an important role in the dynamics of diffuse phase transitions.
Jose Alvarezramirez - One of the best experts on this subject based on the ideXlab platform.
-
inertial effects of adsorbed glycerol monostearate crystals on the shear rheology of water canola oil interfaces
Journal of Food Engineering, 2014Co-Authors: H Carrillonavas, B Fouconnier, C Perezalonso, E J Vernoncarter, Jose AlvarezramirezAbstract:Abstract Glycerol monostearate (GMS) in canola oil dispersions (1.0%, 2.0%, and 3.0% w/w) were cooled down from 70 to 30 °C at a rate of 10.0 °C/min forming CD 1.0 , CD 2.0 , and CD 3.0 crystal dispersions. Interfaces were prepared by pouring CDs over water, and were subjected to a constant shear stress. The creep compliance-time response of the interfaces depended on CD concentration, interfacial film aging time, and shear stress application time. Interfacial rheology experimental data were described by a nearly instantaneous response followed by an exponentially decaying function with two Relaxation Modes, the latter related to Kevin–Voigt elements connected serially involving inertial effects at relatively short times. The faster Relaxation Mode was related to the formation of a two-dimensional solid-like structure, while the slower Relaxation Mode was attributed slow crystal adsorption–desorption diffusional effects in the interface vicinity. The inertial effects had important influence on the interfacial rheology response.