Role of intramolecular interactions in Raman spectra of N 2 and O 2 molecules

2002 ◽  
Author(s):  
Michail A. Buldakov ◽  
Victor N. Cherepanov ◽  
Boris V. Korolev ◽  
Ivan I. Matrosov
Keyword(s):  
Raman Spectra ◽  
Intramolecular Interactions

Role of intramolecular interactions in Raman spectra of N2 and O2 molecules

2003 ◽  
Vol 217 (1) ◽  
pp. 1-8 ◽  
Author(s):  
M.A. Buldakov ◽  
V.N. Cherepanov ◽  
B.V. Korolev ◽  
I.I. Matrosov
Keyword(s):  
Raman Spectra ◽  
Intramolecular Interactions

scholarly journals The role of intramolecular interactions in the functional control of multiheme cytochromesc

FEBS Letters ◽  
2011 ◽  
Vol 586 (5) ◽  
pp. 504-509 ◽  
Author(s):  
Bruno M. Fonseca ◽  
Catarina M. Paquete ◽  
Carlos A. Salgueiro ◽  
Ricardo O. Louro
Keyword(s):  
Intramolecular Interactions ◽  
Functional Control

scholarly journals Conformational Analysis of CmH2m+1OCH2CH2OH (m = 1-4): The Role of CH.cntdot..cntdot..cntdot.O Intramolecular Interactions

1995 ◽  
Vol 99 (20) ◽  
pp. 8066-8070 ◽  
Author(s):  
Francisco P. S. C. Gil ◽  
A. M. Amorim Da Costa ◽  
J. J. C. Teixeira-Dias
Keyword(s):  
Conformational Analysis ◽  
Intramolecular Interactions

scholarly journals Corrigendum to “The role of intramolecular interactions in the functional control of multiheme cytochromesc” [FEBS Lett. 586 (2012) 504-509]

FEBS Letters ◽  
2012 ◽  
Vol 586 (19) ◽  
pp. 3536-3536
Author(s):  
Bruno M. Fonseca ◽  
Catarina M. Paquete ◽  
Carlos A. Salgueiro ◽  
Ricardo O. Louro
Keyword(s):  
Intramolecular Interactions ◽  
Functional Control

scholarly journals Graphene Domain Signature of Raman Spectra of sp2 Amorphous Carbons

Nanomaterials ◽  
2020 ◽  
Vol 10 (10) ◽  
pp. 2021
Author(s):  
Elena F. Sheka ◽  
Yevgeny A. Golubev ◽  
Nadezhda A. Popova
Keyword(s):  
Raman Spectra ◽  
Molecular Spectroscopy ◽  
Basic Structure ◽  
Quasi Particle ◽  
Phonon Spectra ◽  
2D Pattern ◽  
Density Delocalization ◽  
Electron Density Delocalization ◽  
High Degree

The standard D-G-2D pattern of Raman spectra of sp2 amorphous carbons is considered from the viewpoint of graphene domains presenting their basic structure units (BSUs) in terms of molecular spectroscopy. The molecular approximation allows connecting the characteristic D-G doublet spectra image of one-phonon spectra with a considerable dispersion of the C=C bond lengths within graphene domains, governed by size, heteroatom necklace of BSUs as well as BSUs packing. The interpretation of 2D two-phonon spectra reveals a particular role of electrical anharmonicity in the spectra formation and attributes this effect to a high degree of the electron density delocalization in graphene domains. A size-stimulated transition from molecular to quasi-particle phonon consideration of Raman spectra was experimentally traced, which allowed evaluation of a free path of optical phonons in graphene crystal.

scholarly journals Progressive Phosphorylation Modulates the Self-Association of a Variably Modified Histone H3 Peptide

2021 ◽  
Vol 8 ◽  
Author(s):  
George V. Papamokos ◽  
George Tziatzos ◽  
Dimitrios G. Papageorgiou ◽  
Spyros Georgatos ◽  
Efthimios Kaxiras ◽  
...  
Keyword(s):  
Intrinsically Disordered Proteins ◽  
Histone H3 ◽  
Intramolecular Interactions ◽  
Disordered Proteins ◽  
Post Translational Modifications ◽  
Intrinsically Disordered ◽  
Self Association ◽  
Dynamics Simulations ◽  
Peptide Charge

Protein phosphorylation is a key regulatory mechanism in eukaryotic cells. In the intrinsically disordered histone tails, phosphorylation is often a part of combinatorial post-translational modifications and an integral part of the “histone code” that regulates gene expression. Here, we study the association between two histone H3 tail peptides modified to different degrees, using fully atomistic molecular dynamics simulations. Assuming that the initial conformations are either α-helical or fully extended, we compare the propensity of the two peptides to associate with one another when both are unmodified, one modified and the other unmodified, or both modified. The simulations lead to the identification of distinct inter- and intramolecular interactions in the peptide dimer, highlighting a prominent role of a fine-tuned phosphorylation rheostat in peptide association. Progressive phosphorylation appears to modulate peptide charge, inducing strong and specific intermolecular interactions between the monomers, which do not result in the formation of amorphous or ordered aggregates, as documented by experimental evidence derived from Circular Dichroism and NMR spectroscopy. However, upon complete saturation of positive charges by phosphate groups, this effect is reversed: intramolecular interactions prevail and dimerization of zero-charge peptides is markedly reduced. These findings underscore the role of phosphorylation thresholds in the dynamics of intrinsically disordered proteins. Phosphorylation rheostats might account for the divergent effects of histone modifications on the modulation of chromatin structure.

The projection domain of MAP2b regulates microtubule protrusion and process formation in Sf9 cells

2002 ◽  
Vol 115 (7) ◽  
pp. 1523-1539 ◽  
Author(s):  
Dave Bélanger ◽  
Carole Abi Farah ◽  
Minh Dang Nguyen ◽  
Michel Lauzon ◽  
Sylvie Cornibert ◽  
...  
Keyword(s):  
Cell Surface ◽  
Binding Domain ◽  
Intramolecular Interactions ◽  
Microtubule Assembly ◽  
Sf9 Cells ◽  
Microtubule Binding ◽  
Process Formation ◽  
Microtubule Binding Domain ◽  
Projection Domain

The expression of microtubule-associated protein 2 (MAP2), developmentally regulated by alternative splicing, coincides with neurite outgrowth. MAP2 proteins contain a microtubule-binding domain (C-terminal) that promotes microtubule assembly and a poorly characterized domain, the projection domain(N-terminal), extending at the surface of microtubules. MAP2b differs from MAP2c by an additional sequence of 1372 amino acids in the projection domain. In this study, we examined the role of the projection domain in the protrusion of microtubules from the cell surface and the subsequent process formation in Sf9 cells. In this system, MAP2b has a lower capacity to induce process formation than MAP2c. To investigate the role of the projection domain in this event, we expressed truncated forms of MAP2b and MAP2c that have partial or complete deletion of their projection domain in Sf9 cells. Our results indicate that process formation is induced by the microtubule-binding domain of these MAP2 proteins and is regulated by their projection domain. Furthermore, the microtubule-binding activity of MAP2b and MAP2c truncated forms as well as the structural properties of the microtubule bundles induced by them do not seem to be the only determinants that control the protrusion of microtubules from the cell surface in Sf9 cells. Rather, our data suggest that microtubule protrusion and process formation are regulated by intramolecular interactions between the projection domain and its microtubule-binding domain in MAP2b.

Critical Role of Tricyclic Bridges Including Neighboring Rings for Understanding Raman Spectra of Zeolites

2019 ◽  
Vol 141 (51) ◽  
pp. 20318-20324 ◽  
Author(s):  
Tongkun Wang ◽  
Song Luo ◽  
Geoffrey A. Tompsett ◽  
Michael T. Timko ◽  
Wei Fan ◽  
...  
Keyword(s):  
Raman Spectra ◽  
Critical Role

The Role of Fermi and Darling–Dennison Resonances in the Formation of the Raman Spectra of Water and Water–Ethanol Solutions

2019 ◽  
Vol 83 (3) ◽  
pp. 324-329 ◽  
Author(s):  
I. V. Plastinin ◽  
S. A. Burikov ◽  
S. A. Dolenko ◽  
T. A. Dolenko
Keyword(s):  
Raman Spectra

Structural insights into the role of the Chl4–Iml3 complex in kinetochore assembly

2013 ◽  
Vol 69 (12) ◽  
pp. 2412-2419 ◽  
Author(s):  
Qiong Guo ◽  
Yuyong Tao ◽  
Hejun Liu ◽  
Maikun Teng ◽  
Xu Li
Keyword(s):  
De Novo ◽  
Molecular Level ◽  
Structural Information ◽  
Binding Activity ◽  
Intramolecular Interactions ◽  
Exact Role ◽  
Dna Binding Activity ◽  
Kinetochore Assembly ◽  
Structural Insights

Human CENP-N and CENP-L have been reported to selectively recognize the CENP-A nucleosome and to contribute to recruiting other constitutive centromere-associated network (CCAN) complexes involved in assembly of the inner kinetochore. As their homologues, Chl4 and Iml3 from budding yeast function in a similar way inde novoassembly of the kinetochore. A lack of biochemical and structural information precludes further understanding of their exact role at the molecular level. Here, the crystal structure of Iml3 is presented and the structure shows that Iml3 adopts an elongated conformation with a series of intramolecular interactions. Pull-down assays revealed that the C-terminal domain of Chl4, which forms a dimer in solution, is responsible for Iml3 binding. Acting as a heterodimer, the Chl4–Iml3 complex exhibits a low-affinity nonspecific DNA-binding activity which may play an important role in the kinetochore-assembly process.

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