Folding and Unfolding of an Elastinlike Oligopeptide: “Inverse Temperature Transition,” Reentrance, and Hydrogen-Bond Dynamics

Schreiner, Eduard; Nicolini, Chiara; Ludolph, Björn; Ravindra, Revanur; Otte, Nikolaj; Kohlmeyer, Axel; Rousseau, Roger; Winter, Roland; Marx, Dominik

doi:10.1103/physrevlett.92.148101

Cited by 63 publications

(101 citation statements)

References 29 publications

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“…Such a shift between the populations of two different conformers has already been observed in previous MD simulations of the trans ELP and could be correlated with the temperature dependent changes in the dynamics of the peptide and the HB network between the peptide and its solvation shell. [3,22,23] The present study extends these findings by providing an insight into the role of the cis and trans isomers of the proline peptide bond at the ITT. With increasing temperature, the additional thermal energy lowers the free energy barrier of proline isomerization and allows a shift in the trans-cis equilibrium away from one form into the other.…”

Section: Discussionsupporting

confidence: 53%

“…[21] The aim of this work is to continue the theoretical studies carried out previously on the minimal ELP model GVGA C H T U N G T R E N N U N G (VPGVG) in refs. [3,22,23] and substantiate them with experimental NMR data. These studies predict this ELP to undergo a conformational transition from an open ("unfolded") to a closed ("folded") state upon heating in the vein of the ITT scenario.…”

Section: Introductionmentioning

confidence: 70%

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Conformational Dynamics of Minimal Elastin‐Like Polypeptides: The Role of Proline Revealed by Molecular Dynamics and Nuclear Magnetic Resonance

et al. 2008

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Previous molecular dynamics studies of the elastin-like peptide (ELP) GVG(VPGVG) predict that this ELP undergoes a conformational transition from an open to a more compact closed state upon an increase in temperature. These structural changes occurring in this minimal elastin model at the so-called inverse temperature transition (ITT), which takes place when elastin is heated to temperatures of about 20-40 (omicron)C, are investigated further in this work by means of a combined theoretical and experimental approach. To do this, additional extensive classical molecular dynamics (MD) simulations of the capped octapeptide are carried out, analyzed, and compared to data obtained from homonuclear magnetic resonance (NMR) spectroscopy of the same octapeptide. Moreover, in the previous simulations, the proline residue in the ELP is found to act as a hinge, thereby allowing for the large-amplitude opening and closing conformational motion of the ITT. To explore the role of proline in such elastin repeating units, a point mutant (P5I), which replaces the proline residue with an isoleucine residue, is also investigated using the aforementioned theoretical and experimental techniques. The results show that the site-directed mutation completely alters the properties of this ELP, thus confirming the importance of the highly conserved proline residue in the ITT. Furthermore, a correlation between the two different methods employed is seen. Both methods predict the mutant ELP to be present in an unstructured form and the wild type ELP to have a beta-turn-like structure. Finally, the role of the peptidyl cis to trans isomerization of the proline hinge is assessed in detail.

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Section: Discussionsupporting

confidence: 53%

Section: Introductionmentioning

confidence: 70%

Conformational Dynamics of Minimal Elastin‐Like Polypeptides: The Role of Proline Revealed by Molecular Dynamics and Nuclear Magnetic Resonance

et al. 2008

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“…The correlations between hydrogen bond fluctuations and spectral diffusion of aqueous systems have been a topic of tremendous current interest both experimentally [32][33][34][35][36] and theoretically. [37][38][39][40] Here we study such correlations for interfacial molecules by using the so-called population correlation function method [41][42][43][44][45][46][47] for hydrogen bond dynamics and frequency correlation approach 37-40 for spectral diffusion. To the best of our knowledge, such a first principles study of the correlations between the dynamics of hydrogen bonds and frequency fluctuations is presented here for the first time for a liquid-vapor interfacial system.…”

Section: Introductionmentioning

confidence: 99%

Hydrogen bonded structure and dynamics of liquid-vapor interface of water-ammonia mixture: An ab initio molecular dynamics study

Chakraborty

Chandra

2011

The Journal of Chemical Physics

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We have carried out ab initio molecular dynamics simulations of a liquid-vapor interfacial system consisting of a mixture of water and ammonia molecules. We have made a detailed analysis of the structural and dynamical properties of the bulk and interfacial regions of the mixture. Among structural properties, we have looked at the inhomogeneous density profiles of water and ammonia molecules, hydrogen bond distributions, orientational profiles, and also vibrational frequency distributions of bulk and interfacial molecules. It is found that the interfacial molecules show preference for specific orientations so as to form water-ammonia hydrogen bonds at the interface with ammonia as the acceptor. The structure of the system is also investigated in terms of inter-atomic voids present in the system. Among the dynamical properties, we have calculated the diffusion, orientational relaxation, hydrogen bond dynamics, and vibrational spectral diffusion in bulk and interfacial regions. It is found that the diffusion and orientation relaxation of the interfacial molecules are faster than those of the bulk. However, the hydrogen bond lifetimes are longer at the interface which can be correlated with the time scales found from the decay of frequency time correlations.

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“…A number of studies analyzed the origin of the characteristic elastic properties of this protein [28][29][30][31][32]. Dielectric measurements focusing on the hydration dependence showed an onset of protein dynamics at a hydration level of~0.25 g/g, corresponding to~1.2 water molecules per elastin residue [33].…”

Section: Introductionmentioning

confidence: 99%

Effects of solvent concentration and composition on protein dynamics: 13 C MAS NMR studies of elastin in glycerol–water mixtures

Demuth

Haase

Malzacher

et al. 2015

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Folding and Unfolding of an Elastinlike Oligopeptide: “Inverse Temperature Transition,” Reentrance, and Hydrogen-Bond Dynamics

Cited by 63 publications

References 29 publications

Conformational Dynamics of Minimal Elastin‐Like Polypeptides: The Role of Proline Revealed by Molecular Dynamics and Nuclear Magnetic Resonance

Conformational Dynamics of Minimal Elastin‐Like Polypeptides: The Role of Proline Revealed by Molecular Dynamics and Nuclear Magnetic Resonance

Hydrogen bonded structure and dynamics of liquid-vapor interface of water-ammonia mixture: An ab initio molecular dynamics study

Effects of solvent concentration and composition on protein dynamics: 13 C MAS NMR studies of elastin in glycerol–water mixtures

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