LOOKING INTO THE ENERGY LANDSCAPE OF MYOGLOBIN

Using the haem group of myoglobin as a probe in optical experiments makes it possible to study its conformational fluctuations in real time. Results of these experiments can be directly interpreted in terms of the structure of the potential energy surface of the protein. The current view is that proteins have rough energy landscapes comprising a large number of minima which represent conformational substates, and that these substates are hierarchically organized. Here, we show that the energy landscape is characterized by a number of discrete distributions of;barrier heights each representing a tier within a hierarchy of conformational substates. Furthermore, we provide evidence that the energy surface is self-similar and offer suggestions for a characterization of the protein fluctuations

External Inversion, Internal Inversion, and Reflection Invariance

Having in mind that physical systems have different levels of structure we develop the concept of external, internal and total improper Lorentz transformation (space inversion and time reversal). A particle obtained from the ordinary one by the application of internal space inversion or time reversal is generally a different particle. From this point of view the intrinsic parity of a nuclear particle (`elementary particle') is in fact the external intrinsic parity, if we take into account the internal structure of a particle. We show that non-conservation of the external parity does not necessarily imply non-invariance of nature under space inversion. The conventional theory of beta-decay can be corrected by including the internal degrees of freedom to become invariant under total space inversion, though not under the external one.Comment: 15 pages. An early proposal of "mirror matter", published in 1974. This is an exact copy of the published paper. I am posting it here because of the increasing interest in the "exact parity models" and its experimental consequence

Structurally specific thermal fluctuations identify functional sites for DNA transcription

We report results showing that thermally-induced openings of double stranded DNA coincide with the location of functionally relevant sites for transcription. Investigating both viral and bacterial DNA gene promoter segments, we found that the most probable opening occurs at the transcription start site. Minor openings appear to be related to other regulatory sites. Our results suggest that coherent thermal fluctuations play an important role in the initiation of transcription. Essential elements of the dynamics, in addition to sequence specificity, are nonlinearity and entropy, provided by local base-pair constraints

Anomalous relaxation and self-organization in non-equilibrium processes

We study thermal relaxation in ordered arrays of coupled nonlinear elements with external driving. We find, that our model exhibits dynamic self-organization manifested in a universal stretched-exponential form of relaxation. We identify two types of self-organization, cooperative and anti-cooperative, which lead to fast and slow relaxation, respectively. We give a qualitative explanation for the behavior of the stretched exponent in different parameter ranges. We emphasize that this is a system exhibiting stretched-exponential relaxation without explicit disorder or frustration.Comment: submitted to PR

Heat exchange between two interacting nanoparticles beyond the fluctuation-dissipation regime

We show that the observed non-monotonic behavior of the thermal conductance between two nanoparticles when they are brought into contact is originated by an intricate phase space dynamics. Here it is assumed that this dynamics results from the thermally activated jumping through a rough energy landscape. A hierarchy of relaxation times plays the key role in the description of this complex phase space behaviour. Our theory enables us to analyze the heat transfer just before and at the moment of contact.Comment: 4 pages, 1 figure, approved for publication in Physical Review Letter

Fractal Analysis of Protein Potential Energy Landscapes

The fractal properties of the total potential energy V as a function of time t are studied for a number of systems, including realistic models of proteins (PPT, BPTI and myoglobin). The fractal dimension of V(t), characterized by the exponent \gamma, is almost independent of temperature and increases with time, more slowly the larger the protein. Perhaps the most striking observation of this study is the apparent universality of the fractal dimension, which depends only weakly on the type of molecular system. We explain this behavior by assuming that fractality is caused by a self-generated dynamical noise, a consequence of intermode coupling due to anharmonicity. Global topological features of the potential energy landscape are found to have little effect on the observed fractal behavior.Comment: 17 pages, single spaced, including 12 figure

The Goldbeter-Koshland switch in the first-order region and its response to dynamic disorder

In their classical work (Proc. Natl. Acad. Sci. USA, 1981, 78:6840-6844), Goldbeter and Koshland mathematically analyzed a reversible covalent modification system which is highly sensitive to the concentration of effectors. Its signal-response curve appears sigmoidal, constituting a biochemical switch. However, the switch behavior only emerges in the "zero-order region", i.e. when the signal molecule concentration is much lower than that of the substrate it modifies. In this work we showed that the switching behavior can also occur under comparable concentrations of signals and substrates, provided that the signal molecules catalyze the modification reaction in cooperation. We also studied the effect of dynamic disorders on the proposed biochemical switch, in which the enzymatic reaction rates, instead of constant, appear as stochastic functions of time. We showed that the system is robust to dynamic disorder at bulk concentration. But if the dynamic disorder is quasi-static, large fluctuations of the switch response behavior may be observed at low concentrations. Such fluctuation is relevant to many biological functions. It can be reduced by either increasing the conformation interconversion rate of the protein, or correlating the enzymatic reaction rates in the network.Comment: 23 pages, 4 figures, accepted by PLOS ON

Reaction rate for two--neutron capture by 4^4He

Recent investigations suggest that the neutrino--heated hot bubble between the nascent neutron star and the overlying stellar mantle of a type--II supernova may be the site of the r--process. In the preceding $\alpha$--process building up the elements to $A \approx 100$, the $^4$He(2n,$\gamma$)$^6$He-- and $^6$He($\alpha$,n)$^9$Be--reactions bridging the instability gap at $A=5$ and $A=8$ could be of relevance. We suggest a mechanism for $^4$He(2n,$\gamma$)$^6$He and calculate the reaction rate within the $\alpha$+n+n approach. The value obtained is about a factor 1.6 smaller than the one obtained recently in the simpler direct--capture model, but is at least three order of magnitude enhanced compared to the previously adopted value. Our calculation confirms the result of the direct--capture calculation that under representative conditions in the $\alpha$--process the reaction path proceeding through $^6$He is negligible compared to $^4$He($\alpha$n,$\gamma$)$^9$Be.Comment: 13 pages, 4 postscript figures, to appear in "Zeitschrift f. Physik A", changed internet address and filename, the uuencoded postscript file including the figures is available at ftp://is1.kph.tuwien.ac.at/pub/ohu/twoneutron.u