اشترك بالحزمة الذهبية واحصل على وصول غير محدود شمرا أكاديميا
تسجيل مستخدم جديدBlue Emission in Proteins
132
0
0.0
(
0
)
اسأل ChatGPT حول البحث
ﻻ يوجد ملخص باللغة العربية
Recent literatures reported blue-green emission from amyloid fibril as exclusive signature of fibril formation. This unusual visible luminescence is regularly used to monitor fibril growth. Blue-green emission has also been observed in crystalline protein and in solution. However, the origin of this emission is not known exactly. Our spectroscopic study of serum proteins reveals that the blue-green emission is a property of protein monomer. Evidences suggest that semiconductor-like band structure of proteins with the optical band-gap in the visible region is possibly the origin of this phenomenon. We show here that the band structure of proteins is primarily the result of electron delocalization through the peptide chain, rather than through the hydrogen bond network in secondary structure.
قيم البحث
اقرأ أيضاً
The convergent interests of different scientific disciplines, from biochemistry to electronics, toward the investigation of protein electrical properties, has promoted the development of a novel bailiwick, the so called proteotronics. The main aim of
proteotronics is to propose and achieve innovative electronic devices, based on the selective action of specific proteins. This paper gives a sketch of the fields of applications of proteotronics, by using as significant example the detection of a specific odorant molecule carried out by an olfactory receptor. The experiment is briefly reviewed and its theoretical interpretation given. Further experiments are envisioned and expected results discussed in the perspective of an experimental validation.
We explore the dynamical large-deviations of a lattice heteropolymer model of a protein by means of path sampling of trajectories. We uncover the existence of non-equilibrium dynamical phase-transitions in ensembles of trajectories between active and
inactive dynamical phases, whose nature depends on properties of the interaction potential. When the full heterogeneity of interactions due to the amino-acid sequence is preserved, as in a fully interacting model or in a heterogeneous version of the G={o} model where only native interactions are considered, the transition is between the equilibrium native state and a highly native but kinetically trapped state. In contrast, for the homogeneous G={o} model, where there is a single native energy and the sequence plays no role, the dynamical transition is a direct consequence of the static bi-stability between unfolded and native states. In the heterogeneous case the native-active and native-inactive states, despite their static similarity, have widely varying dynamical properties, and the transition between them occurs even in lattice proteins whose sequences are designed to make them optimal folders.
A theoretical analysis of the unfolding pathway of simple modular proteins in length- controlled pulling experiments is put forward. Within this framework, we predict the first module to unfold in a chain of identical units, emphasizing the ranges of
pulling speeds in which we expect our theory to hold. These theoretical predictions are checked by means of steered molecular dynamics of a simple construct, specifically a chain composed of two coiled-coils motives, where anisotropic features are revealed. These simulations also allow us to give an estimate for the range of pulling velocities in which our theoretical approach is valid.
We report on the successful synthesis and hyperpolarization of N unprotected {alpha} amino acid ethyl acrylate esters and extensively, on an alanine derivative hyperpolarized by PHIP (4.4$pm$1% $^{13}$C-polarization), meeting required levels for in v
ivo detection. Using water as solvent increases biocompatibility and the absence of N-protection is expected to maintain biological activity.
We demonstrate that the coupling of excitonic and vibrational motion in biological complexes can provide mechanisms to explain the long-lived oscillations that have been obtained in non linear spectroscopic signals of different photosynthetic pigment
protein complexes and we discuss the contributions of excitonic versus purely vibrational components to these oscillatory features. Considering a dimer model coupled to a structured spectral density we exemplify the fundamental aspects of the electron-phonon dynamics, and by analyzing separately the different contributions to the non linear signal, we show that for realistic parameter regimes purely electronic coherence is of the same order as purely vibrational coherence in the electronic ground state. Moreover, we demonstrate how the latter relies upon the excitonic interaction to manifest. These results link recently proposed microscopic, non-equilibrium mechanisms to support long lived coherence at ambient temperatures with actual experimental observations of oscillatory behaviour using 2D photon echo techniques to corroborate the fundamental importance of the interplay of electronic and vibrational degrees of freedom in the dynamics of light harvesting aggregates.
سجل دخول لتتمكن من نشر تعليقات
التعليقات
جاري جلب التعليقات
سجل دخول لتتمكن من متابعة معايير البحث التي قمت باختيارها
