Structural and conformational changes during thermally-induced crystallization of poly(trimethylene terephthalate) by infrared spectroscopy

2008 ◽  
Vol 46 (14) ◽  
pp. 1497-1504 ◽  
Author(s):  
Mustafa Yamen ◽  
Sabahattin Ozkaya ◽  
Nadarajah Vasanthan
Keyword(s):  
Infrared Spectroscopy ◽  
Conformational Changes ◽  
Thermally Induced ◽  
Trimethylene Terephthalate ◽  
Induced Crystallization

The influence of Fe3+ doping on thermally induced crystallization and phase evolution of amorphous calcium phosphate

CrystEngComm ◽  
2021 ◽  
Author(s):  
Diana Griesiute ◽  
Lauryna Sinusaite ◽  
Agne Kizalaite ◽  
Andris Antuzevics ◽  
Kestutis Mazeika ◽  
...  
Keyword(s):  
Calcium Phosphate ◽  
Amorphous Calcium Phosphate ◽  
Phase Evolution ◽  
Thermally Induced ◽  
Induced Crystallization

The present study investigates thermally induced crystallization and phase evolution of amorphous calcium phosphate (ACP) partially substituted with Fe3+ ions (M/P = 1.5 : 1). It was demonstrated that the...

scholarly journals The effects of Ca2+ and Cd2+ on the secondary and tertiary structure of bovine testis calmodulin. A circular-dichroism study

1986 ◽  
Vol 238 (2) ◽  
pp. 485-490 ◽  
Author(s):  
S R Martin ◽  
P M Bayley
Keyword(s):  
Circular Dichroism ◽  
Conformational Changes ◽  
Metal Ion ◽  
Tertiary Structure ◽  
Thermal Unfolding ◽  
Apparent Effect ◽  
Thermally Induced ◽  
Circular Dichroïsm ◽  
Secondary And Tertiary Structure

Near-u.v. and far-u.v. c.d. spectra of bovine testis calmodulin and its tryptic fragments (TR1C, N-terminal half, residues 1-77, and TR2C, C-terminal half, residues 78-148) were recorded in metal-ion-free buffer and in the presence of saturating concentrations of Ca2+ or Cd2+ under a range of different solvent conditions. The results show the following: if there is any interaction between the N-terminal and C-terminal halves of calmodulin, it has not apparent effect on the secondary or tertiary structure of either half; the conformational changes induced by Ca2+ or Cd2+ are substantially greater in TR2C than they are in TR1C; the presence of Ca2+ or Cd2+ confers considerable stability with respect to urea-induced denaturation, both for the whole molecule and for either of the tryptic fragments; a thermally induced transition occurs in whole calmodulin at temperatures substantially below the temperature of major thermal unfolding, both in the presence and in the absence of added metal ion; the effects of Cd2+ are identical with those of Ca2+ under all conditions studied.

scholarly journals Conformational Changes Generated in GroEL during ATP Hydrolysis as Seen by Time-resolved Infrared Spectroscopy

1999 ◽  
Vol 274 (9) ◽  
pp. 5508-5513 ◽  
Author(s):  
Frithjof von Germar ◽  
Asier Galán ◽  
Oscar Llorca ◽  
Jose L. Carrascosa ◽  
Jose M. Valpuesta ◽  
...  
Keyword(s):  
Infrared Spectroscopy ◽  
Conformational Changes ◽  
Atp Hydrolysis ◽  
Time Resolved ◽  
Time Resolved Infrared Spectroscopy

Circular Dichroism of C-Phycoerythrin: A Conformational Analysis

1980 ◽  
Vol 35 (5-6) ◽  
pp. 367-375 ◽  
Author(s):  
Elisabeth Langer ◽  
Harald Lehner ◽  
Wolfhart Rüdiger ◽  
Barbara Zickendraht-Wendelstadt
Keyword(s):  
Circular Dichroism ◽  
Secondary Structure ◽  
Conformational Changes ◽  
Spectral Region ◽  
Protein Unfolding ◽  
Extensive Study ◽  
Random Coil ◽  
Linear Superposition ◽  
Thermally Induced ◽  
Circular Dichroïsm

Abstract An extensive study of the chiroptical properties of C-phycoerythrin and the α-and β-subunits in the spectral region from 700 -200 nm is presented. Based on the VIS-circular dichroism inherently chiral conform ations are proposed for the co­ valently linked chromophores. By means of mean residue ellipticities and the experimental circular dichroism spectra in the region of the n → π* peptide transition the a-helix contents of the apoproteins of the ac-and ß-subunits are estimated to amount to 60% and 40%, respectively. The circular dichroism spectrum of native C-phycoerythrin is congruent with a linear superposition of the α-and β-subspectra, in the whole spectral region studied. Since a-and β-subunits are associated in native C-phycoery-thrin as revealed by sedim entation analysis the interactions between the subunits in the native chromoprotein are not accom panied by substantial conform ational changes. In the temperature range 0°-40°C the thermally induced changes of the chrom ophores in native C-phycoerythrin are not associated with changes of the secondary structure of the apoprotein. Unfolding occurs at 60°-70°C but slowly leads to irreversible denaturation. Protein unfolding starts at 3 M urea. The random coil secondary structure of the apoproteins is reached at 8 M urea. At this concentration the absorbance and the optical activity of the chrom o­ phores are reduced by a factor 3 and 10, respectively. The conformational changes in the peptide with increasing denaturant concentration are not synchronous with those induced in the Chromo­ phore indicating that a m ultistep process is operative during unfolding. The C D results on dena­ turation are supplem ented by absorption and em ission spectroscopy.

Preparation of levodopa-loaded crystalsomes through thermally induced crystallization reverses functional deficits in Parkinsonian mice

2019 ◽  
Vol 7 (4) ◽  
pp. 1623-1631 ◽  
Author(s):  
Xinyu Li ◽  
Qianqian Liu ◽  
Dashuai Zhu ◽  
Yongzhe Che ◽  
Xizeng Feng
Keyword(s):  
Pathological Features ◽  
Thermally Induced ◽  
Functional Deficits ◽  
Behavioral Impairments ◽  
Induced Crystallization

The prepared levodopa loaded crystalsomes are nanoscale crystals and controlling levodopa release which improving MPTP-induced behavioral impairments and pathological features of mice.

Thermally induced crystallization and phase evolution in powders derived from amorphous calcium phosphate precipitates with a Ca/P ratio of 1:1

2016 ◽  
Vol 450 ◽  
pp. 190-196 ◽  
Author(s):  
Zoltan Zyman ◽  
Matthias Epple ◽  
Anton Goncharenko ◽  
Dmytro Rokhmistrov ◽  
Oleg Prymak ◽  
...  
Keyword(s):  
Calcium Phosphate ◽  
Amorphous Calcium Phosphate ◽  
Phase Evolution ◽  
Thermally Induced ◽  
Induced Crystallization

scholarly journals Thermally induced conformational changes and protein–protein interactions of bovine serum albumin in aqueous solution under different pH and ionic strengths as revealed by SAXS measurements

2017 ◽  
Vol 19 (26) ◽  
pp. 17143-17155 ◽  
Author(s):  
Dmitry Molodenskiy ◽  
Evgeny Shirshin ◽  
Tatiana Tikhonova ◽  
Andrey Gruzinov ◽  
Georgy Peters ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Changes ◽  
Interaction Potential ◽  
Protein Interactions ◽  
Bovine Serum ◽  
Protein Protein Interactions ◽  
Thermally Induced ◽  
Before And After

Temperature-induced oligomerization of albumin before and after protein melting was studied using SAXS and interpreted in terms of interaction potential.

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