Conditions of spiral domain structure stability

1998 ◽  
Vol 08 (PR2) ◽  
pp. Pr2-393-Pr2-396 ◽  
Author(s):  
Y. A. Mamalui ◽  
K. V. Lamonova ◽  
E. N. Soika
Keyword(s):  
Domain Structure ◽  
Structure Stability ◽  
Spiral Domain

scholarly journals Conserved tryptophan mutation disrupts structure and function of immunoglobulin domain revealing unusual tyrosine fluorescence

2020 ◽  
Author(s):  
Ravi Vattepu ◽  
Rachel A. Klausmeyer ◽  
Allan Ayella ◽  
Rahul Yadav ◽  
Joseph T. Dille ◽  
...  
Keyword(s):  
Cell Line ◽  
Domain Structure ◽  
Cancer Cell ◽  
Cancer Cell Line ◽  
Actin Binding ◽  
Structure Stability ◽  
Hydrophobic Core ◽  
Tyrosine Fluorescence ◽  
And Function ◽  
Ig Domain

ABSTRACTImmunoglobulin (Ig) domains are the most prevalent protein domain structure and share a highly conserved folding pattern; however, this structural family of proteins is also the most diverse in terms of biological roles and tissue expression. Ig domains vary significantly in amino acid sequence but share a highly conserved tryptophan in the hydrophobic core of this beta-stranded protein. Palladin is an actin binding and bundling protein that has five Ig domains and plays an important role in normal cell adhesion and motility. Mutation of the core tryptophan in one Ig domain of palladin has been identified in a pancreatic cancer cell line, suggesting a crucial role for this sole tryptophan in palladin Ig domain structure, stability, and function. We found that actin binding and bundling was not completely abolished with removal of this tryptophan despite a partially unfolded structure and significantly reduced stability of the mutant Ig domain as shown by circular dichroism investigations. In addition, this mutant palladin domain displays a tryptophan-like fluorescence attributed to an anomalous tyrosine emission at 345 nm. Our results indicate that this emission originates from a tyrosinate that may be formed in the excited ground state by proton transfer to a nearby glutamyl residue. Furthermore, this study emphasizes the importance of tryptophan in protein structural stability and illustrates how tyrosinate emission contributions may be overlooked during the interpretation of the fluorescence properties of proteins.SHORT ABSTRACTThis study explores the functional and structural consequences of a point mutation in palladin, an Ig domain protein first identified in a pancreatic tumor cancer cell line. While exploring the consequences of mutating this conserved tryptophan in the hydrophobic core of the most prevalent domain structure found in proteins, an anomalous tyrosine fluorescence phenomenon was exposed.

Domain structure, stability and domain-domaininteractions in recombinant factor XIII

1995 ◽  
Vol 248 (2) ◽  
pp. 414-430 ◽  
Author(s):  
Igor V. Kurochkin ◽  
Roman Procyk ◽  
Paul D. Bishop ◽  
Vivien C. Yee ◽  
David C. Teller ◽  
...  
Keyword(s):  
Domain Structure ◽  
Factor Xiii ◽  
Structure Stability

scholarly journals Domain Structure, Stability and Interactions in Streptokinase

1996 ◽  
Vol 239 (2) ◽  
pp. 333-339 ◽  
Author(s):  
Leonid V. Medved ◽  
Dmitry A. Solovjov ◽  
Kenneth C. Ingham
Keyword(s):  
Domain Structure ◽  
Structure Stability

Domains and domain nucleation in magnetron-sputtered CoCr thin films

1993 ◽  
Vol 51 ◽  
pp. 1046-1047
Author(s):  
B. G. Demczyk
Keyword(s):  
Thin Films ◽  
Domain Structure ◽  
Magnetic Domain ◽  
Domain Size ◽  
Film Plane ◽  
Magnetic Domain Structure ◽  
Perpendicular Magnetization ◽  
Columnar Grains ◽  
Reversal Mechanism ◽  
Lorentz Transmission Electron Microscopy

CoCr thin films have been of interest for a number of years due to their strong perpendicular anisotropy, favoring magnetization normal to the film plane. The microstructure and magnetic properties of CoCr films prepared by both rf and magnetron sputtering have been examined in detail. By comparison, however, relatively few systematic studies of the magnetic domain structure and its relation to the observed film microstructure have been reported. In addition, questions still remain as to the operative magnetization reversal mechanism in different film thickness regimes. In this work, the magnetic domain structure in magnetron sputtered Co-22 at.%Cr thin films of known microstructure were examined by Lorentz transmission electron microscopy. Additionally, domain nucleation studies were undertaken via in-situ heating experiments.It was found that the 50 nm thick films, which are comprised of columnar grains, display a “dot” type domain configuration (Figure 1d), characteristic of a perpendicular magnetization. The domain size was found to be on the order of a few structural columns in diameter.

Ferroelectric Domain Structure of Pb(Zr.52Ti.48)03

1980 ◽  
Vol 38 ◽  
pp. 214-215
Author(s):  
E.K. Goo ◽  
R.K. Mishra
Keyword(s):  
Phase Transformation ◽  
Domain Structure ◽  
Tetragonal Phase ◽  
Ferroelectric Domain ◽  
Cubic Phase ◽  
Ion Milling ◽  
Thin Foils ◽  
Ferroelectric Domain Structure ◽  
Ferroelectric Domains

Ferroelectric domains are twins that are formed when PZT undergoes a phase transformation from a non-ferroelectric cubic phase to a ferroelectric tetragonal phase upon cooling below ∼375°C.,1 The tetragonal phase is spontaneously polarized in the direction of c-axis, making each twin a ferroelectric domain. Thin foils of polycrystalline Pb (Zr.52Ti.48)03 were made by ion milling and observed in the Philips EM301 with a double tilt stage.

Development and Psychometric Evaluation of a Revised Sense of Coherence Scale

2018 ◽  
Vol 34 (3) ◽  
pp. 206-215 ◽  
Author(s):  
Rahel Bachem ◽  
Andreas Maercker
Keyword(s):  
Posttraumatic Growth ◽  
Factor Structure ◽  
Sense Of Coherence ◽  
Psychological Health ◽  
Psychometric Evaluation ◽  
Health Indicators ◽  
Structure Stability ◽  
Confirmatory Factor Analyses ◽  
Reliability Factor ◽  
Two Samples

Abstract. The present study introduces a revised Sense of Coherence (SOC) scale, a new conceptualization and operationalization of the resilience indicator SOC. It outlines the scale development and aims for testing its reliability, factor structure, and validity. Literature on Antonovsky’s SOC (SOC-A) was critically reviewed to identify needs for improving the scale. The scale was investigated in two samples. Sample 1 consisted of 334 bereaved participants, Sample 2 of 157 healthy controls. The revised SOC Scale, SOC-A, and theoretically relevant questionnaires were applied. Explorative and confirmatory factor analyses established a three-factor structure in both samples. The revised SOC Scale showed significant but discriminative associations with related constructs, including self-efficacy, posttraumatic growth, and neuroticism. The revised measure was significantly associated with psychological health indicators, including persistent grief, depression, and anxiety, but not to the extent as the previous SOC-A. Stability over time was sufficient. The study provides psychometric support for the revised SOC conceptualization and scale. It has several advantages over the previous SOC-A scale (unique variance, distinct factor structure, stability). The scale could be used for clinical and health psychological testing or research into the growing field of studies on resilience over the life span.

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