An investigation on percutaneous permeation of flurbiprofen enantiomers: The role of molecular interaction between drug and skin components

Observations have been made on the role of a divalent cation (calcium ion) during OsO4 fixation of nuclei of frog erythrocytes, mainly after isolation from cells. The volume of the nucleus depends partly on the molecular interaction of charged macromolecules, is controlled by the ionic strength of the medium, and hence may be used as a guide in attempts to preserve structure. When the isolation and fixation media contain 0.01 M calcium at pH 6.3 the volume changes, in the light microscope, during processing are small. When the fixative does not contain these ions, reversible volume changes occur during fixation and dehydration. The chromatin of nuclei processed with minimal volume change appears, in the electron microscope, to contain fine dots and lines about 20 to 40 A in diameter, relatively close together. The chromatin structure of nuclei in which volume changes have occurred consists of dense irregularly shaped patches, relatively far apart, and ranging in diameter from about 200 A down to the limits of visibility (20 to 30 A). It is suggested that the latter structure is a precipitation artefact.

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Elucidating the molecular interaction of serum albumin with nizatidine and the role of β-cyclodextrin: multi-spectroscopic and computational approach

Journal of Biomolecular Structure and Dynamics ◽

10.1080/07391102.2019.1604265 ◽

2019 ◽

Vol 38 (5) ◽

pp. 1375-1387 ◽

Cited By ~ 2

Author(s):

Yusra Rahman ◽

Shumaila Afrin ◽

Mustafa Alhaji Isa ◽

Shahbaz Ahmed ◽

Mohammad Tabish

Keyword(s):

Serum Albumin ◽

Molecular Interaction ◽

Computational Approach

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Nanostructured polyolefins/clay composites: role of the molecular interaction at the interface

Polymers for Advanced Technologies ◽

10.1002/pat.1107 ◽

2008 ◽

Vol 19 (6) ◽

pp. 560-568 ◽

Cited By ~ 24

Author(s):

Elisa Passaglia ◽

Monica Bertoldo ◽

Serena Coiai ◽

Sylvain Augier ◽

Stefania Savi ◽

...

Keyword(s):

Molecular Interaction

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2P279 1A1520 Role of aromatic residue for inter-molecular interaction between bacteriorhodopsin trimer studied by high-speed AFM(The 48th Annual Meeting of the Biophysical Society of Japan)

Seibutsu Butsuri ◽

10.2142/biophys.50.s132_1 ◽

2010 ◽

Vol 50 (supplement2) ◽

pp. S132

Author(s):

Hayato Yamashita ◽

Mikihiro Shibata ◽

Takayuki Uchihashi ◽

Toshio Ando

Keyword(s):

Annual Meeting ◽

Molecular Interaction ◽

High Speed ◽

Aromatic Residue ◽

Biophysical Society

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Reactivities of Actin as a Contractile Protein

The Journal of General Physiology ◽

10.1085/jgp.50.6.119 ◽

1967 ◽

Vol 50 (6) ◽

pp. 119-133 ◽

Cited By ~ 7

Author(s):

Teru Hayashi

Keyword(s):

Complex Formation ◽

Molecular Interaction ◽

Actin Filaments ◽

Molecular Basis ◽

Striated Muscle ◽

Thin Filaments ◽

Contraction Process ◽

Tentative Hypothesis ◽

Myosin Interaction

The molecular basis for the mechanism of contraction in striated muscle, with primary emphasis on the interaction between the thick and thin filaments and the role of the thin (actin) filaments, is the theme presented. Recent information relating to actin-myosin interaction points up the fact that definitive statements cannot be made regarding the molecular interaction(s) that lead to contraction. Nevertheless, the properties of actin indicate that (a) actin in the monomeric state has properties differing markedly from actin in the polymer (filament) state; (b) these property differences may be significant in the contractile process, for they include changes in the reactivity of the bound nucleotide and actin-myosin complex formation; (c) the bound nucleotide seems to be required in the contraction process. For these, and other, reasons discussed, the tentative hypothesis is advanced that the contraction reaction involves local changes in the actin filament providing local monomer or monomer-like actin units in the reaction with myosin.

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