scholarly journals Application of Neutron Scattering in Amino Acid Crystals – Structural and Dynamical Information

10.5772/62198 ◽  
2016 ◽  
Author(s):  
Paulo T. C. Freire ◽  
José E. M. Pereira ◽  
Heloisa N. Bordallo
Keyword(s):  
Amino Acid ◽  
Neutron Scattering ◽  
Dynamical Information

Structure of ionic liquids with amino acid anions via neutron diffraction

RSC Advances ◽  
2015 ◽  
Vol 5 (82) ◽  
pp. 67220-67226 ◽  
Author(s):  
S. E. Norman ◽  
A. H. Turner ◽  
T. G. A. Youngs
Keyword(s):  
Ionic Liquids ◽  
Amino Acid ◽  
Neutron Diffraction ◽  
Neutron Scattering ◽  
Total Neutron

Total neutron scattering studies on amino acid-based ionic liquids reveal significant directional interactions between anions, especially for serinate-derived ions.

Microstructural Characterization of Foam Formed by a Hydroxy Group-Containing Amino Acid Surfactant Using Small-Angle Neutron Scattering

Langmuir ◽  
2020 ◽  
Vol 36 (27) ◽  
pp. 7808-7813
Author(s):  
Shiho Yada ◽  
Hiroshi Shimosegawa ◽  
Hiroya Fujita ◽  
Munehiro Yamada ◽  
Yukako Matsue ◽  
...  
Keyword(s):  
Amino Acid ◽  
Neutron Scattering ◽  
Hydroxy Group ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Microstructural Characterization

The staining pattern of the tropomyosin sequence is displayed in a new paracrystal

1986 ◽  
Vol 44 ◽  
pp. 150-151
Author(s):  
M.K. Lamvik ◽  
L.L. Klatt
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Staining Pattern ◽  
Banding Patterns ◽  
Mass Thickness ◽  
New Form

Tropomyosin paracrystals have been used extensively as test specimens and magnification standards due to their clear periodic banding patterns. The paracrystal type discovered by Ohtsuki1 has been of particular interest as a test of unstained specimens because of alternating bands that differ by 50% in mass thickness. While producing specimens of this type, we came across a new paracrystal form. Since this new form displays aligned tropomyosin molecules without the overlaps that are characteristic of the Ohtsuki-type paracrystal, it presents a staining pattern that corresponds to the amino acid sequence of the molecule.

Electron probe x-ray microanalysis and electron microscopy of amino acid absorption and transport by the small intestine: inhibition by chemical poisons and correlation to the elemental composition of the epithelial cells

1986 ◽  
Vol 44 ◽  
pp. 134-135
Author(s):  
A. J. Tousimis
Keyword(s):  
Small Intestine ◽  
Amino Acid ◽  
Epithelial Cells ◽  
Elemental Composition ◽  
Isotope Labeling ◽  
Structural Components ◽  
X Ray ◽  
Human Small Intestine ◽  
Transport Studies

The elemental composition of amino acids is similar to that of the major structural components of the epithelial cells of the small intestine and other tissues. Therefore, their subcellular localization and concentration measurements are not possible by x-ray microanalysis. Radioactive isotope labeling: I131-tyrosine, Se75-methionine and S35-methionine have been successfully employed in numerous absorption and transport studies. The latter two have been utilized both in vitro and vivo, with similar results in the hamster and human small intestine. Non-radioactive Selenomethionine, since its absorption/transport behavior is assumed to be the same as that of Se75- methionine and S75-methionine could serve as a compound tracer for this amino acid.

Immunoelectron microscope detection of C-type natriuretic peptide in normal human atrial tissue

1993 ◽  
Vol 51 ◽  
pp. 388-389
Author(s):  
Chi-Ming Wei ◽  
Margaret Hukee ◽  
Christopher G.A. McGregor ◽  
John C. Burnett
Keyword(s):  
Amino Acid ◽  
Natriuretic Peptide ◽  
Vascular Tone ◽  
Cardiac Tissue ◽  
Ring Structure ◽  
Terminal Amino Acid ◽  
Amino Acid Peptide ◽  
Normal Human ◽  
Terminal Amino ◽  
The Brain

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.

Local atomic structure of relaxor ferroelectric solids studied by pulsed neutron scattering

1994 ◽  
Vol 52 ◽  
pp. 554-555
Author(s):  
T. Egami ◽  
H. D. Rosenfeld ◽  
S. Teslic
Keyword(s):  
Neutron Scattering ◽  
Atomic Structure ◽  
Argonne National Laboratory ◽  
Relaxor Ferroelectrics ◽  
Relaxor Ferroelectric ◽  
Crystallographic Structure ◽  
Chemical Inhomogeneity ◽  
Distribution Analysis ◽  
Ferroelectric Transition ◽  
Pulsed Neutron

Relaxor ferroelectrics, such as Pb(Mg1/3Nb2/3)O3 (PMN) or (Pb·88La ·12)(Zr·65Ti·35)O3 (PLZT), show diffuse ferroelectric transition which depends upon frequency of the a.c. field. In spite of their wide use in various applications details of their atomic structure and the mechanism of relaxor ferroelectric transition are not sufficiently understood. While their crystallographic structure is cubic perovskite, ABO3, their thermal factors (apparent amplitude of thermal vibration) is quite large, suggesting local displacive disorder due to heterovalent ion mixing. Electron microscopy suggests nano-scale structural as well as chemical inhomogeneity.We have studied the atomic structure of these solids by pulsed neutron scattering using the atomic pair-distribution analysis. The measurements were made at the Intense Pulsed Neutron Source (IPNS) of Argonne National Laboratory. Pulsed neutrons are produced by a pulsed proton beam accelerated to 750 MeV hitting a uranium target at a rate of 30 Hz. Even after moderation by a liquid methane moderator high flux of epithermal neutrons with energies ranging up to few eV’s remain.

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