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Dr. Dean Strotz Dr. Julien Orts Dr. Harindranath Kadavath Dr. Michael Friedmann Dhiman Ghosh Dr. Simon Olsson Dr. Celestine N. Chi Aditya Pokharna Prof. Dr. Peter Güntert Dr. Beat Vögeli Prof. Dr. Roland Riek 《Angewandte Chemie (Weinheim an der Bergstrasse, Germany)》2020,132(49):22316-22323
Protein allostery is a phenomenon involving the long range coupling between two distal sites in a protein. In order to elucidate allostery at atomic resoluion on the ligand-binding WW domain of the enzyme Pin1, multistate structures were calculated from exact nuclear Overhauser effect (eNOE). In its free form, the protein undergoes a microsecond exchange between two states, one of which is predisposed to interact with its parent catalytic domain. In presence of the positive allosteric ligand, the equilibrium between the two states is shifted towards domain–domain interaction, suggesting a population shift model. In contrast, the allostery-suppressing ligand decouples the side-chain arrangement at the inter-domain interface thereby reducing the inter-domain interaction. As such, this mechanism is an example of dynamic allostery. The presented distinct modes of action highlight the power of the interplay between dynamics and function in the biological activity of proteins. 相似文献
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Dr. Harindranath Kadavath Dr. Mariusz Jaremko Dr. Łukasz Jaremko Dr. Jacek Biernat Prof. Dr. Eckhard Mandelkow Prof. Dr. Markus Zweckstetter 《Angewandte Chemie (International ed. in English)》2015,54(35):10347-10351
Microtubules are regulated by microtubule‐associated proteins. However, little is known about the structure of microtubule‐associated proteins in complex with microtubules. Herein we show that the microtubule‐associated protein Tau, which is intrinsically disordered in solution, locally folds into a stable structure upon binding to microtubules. While Tau is highly flexible in solution and adopts a β‐sheet structure in amyloid fibrils, in complex with microtubules the conserved hexapeptides at the beginning of the Tau repeats two and three convert into a hairpin conformation. Thus, binding to microtubules stabilizes a unique conformation in Tau. 相似文献
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Dipankar Chakrabarti Asmita Mukherjee Rajen Kundu A. Harindranath 《Physics letters. [Part B]》2000,480(3-4):409-417
Issues related with microcausality violation and continuum limit in the context of (1+1) dimensional scalar field theory in discretized light-cone quantization (DLCQ) are addressed in parallel with discretized equal time quantization (DETQ) and the fact that Lorentz invariance and microcausality are restored if one can take the continuum limit properly is emphasized. In the free case, it is shown with numerical evidence that the continuum results can be reproduced from DLCQ results for the Pauli–Jordan function and the real part of Feynman propagator. The contributions coming from k+ near zero region in these cases are found to be very small. In the interacting case, aspects related to the continuum limit of DLCQ results in perturbation theory in momentum space are discussed. 相似文献
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Harindranath Kadavath Natalia Cecilia Prymaczok Cédric Eichmann Roland Riek Juan Atilio Gerez 《Angewandte Chemie (International ed. in English)》2023,62(4):e202213976
Governing function, half-life and subcellular localization, the 3D structure and dynamics of proteins are in nature constantly changing in a tightly regulated manner to fulfill the physiological and adaptive requirements of the cells. To find evidence for this hypothesis, we applied in-cell NMR to three folded model proteins and propose that the splitting of cross peaks constitutes an atomic fingerprint of distinct structural states that arise from multiple target binding co-existing inside mammalian cells. These structural states change upon protein loss of function or subcellular localisation into distinct cell compartments. In addition to peak splitting, we observed NMR signal intensity attenuations indicative of transient interactions with other molecules and dynamics on the microsecond to millisecond time scale. 相似文献