Reorientation Motion and Preferential Interactions of a Peptide in Denaturants and Osmolyte

2016 ◽  
Vol 120 (12) ◽  
pp. 3089-3099 ◽  
Author(s):  
Gouri S. Jas ◽  
Eric C. Rentchler ◽  
Agnieszka M. Słowicka ◽  
John R. Hermansen ◽  
Carey K. Johnson ◽  
...  
Keyword(s):  
Preferential Interactions ◽  
Reorientation Motion

scholarly journals Deciphering preferential interactions within supramolecular protein complexes: the proteasome case

2015 ◽  
Vol 11 (1) ◽  
pp. 771 ◽  
Author(s):  
Bertrand Fabre ◽  
Thomas Lambour ◽  
Luc Garrigues ◽  
François Amalric ◽  
Nathalie Vigneron ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Preferential Interactions

35Cl NQR and Crystal Structure Studies of Salts of Chlorodifluoro- and Dichloroacetic Acid

1992 ◽  
Vol 47 (1-2) ◽  
pp. 241-253 ◽  
Author(s):  
Reha Basaran ◽  
Shi-qi Dou ◽  
Alarich Weiss
Keyword(s):  
Crystal Structure ◽  
Lattice Relaxation ◽  
Lattice Relaxation Time ◽  
Dichloroacetic Acid ◽  
Spin Lattice Relaxation ◽  
X Ray Diffraction ◽  
Spin Lattice ◽  
Chlorodifluoroacetic Acid ◽  
Reorientation Motion ◽  
Guanidinium Salt

AbstractThe 35Cl NQR spectra of several chlorodifluoroacetates were studied as a function of temperature, including the acid ClF2CCOOH. The cations were: Ammonium, guanidinium, paramethylanilinium. Also some acid salts M⊕ClF2CCOO⊖ • n - ClF2CCOOH ( n > l ) were studied by 35Cl NQR. The bleaching temperatures of the NQR signals were determined. In the para-methylanilinium salt and in the guanidinium salt a phase transition has been observed. The crystal structure of guanidinium chlorodifluoroacetate has been determined at room temperature (a = 1089 pm, 6 = 845 pm, c = 832 pm, space group Pnma, Z = 4). For comparison, guanidinium dichloroacetate was studied by 35Cl NQR and by X-ray diffraction, too: P21/c, Z = 4 , a = 804pm, b = 1202 pm, c = 1080 pm, ß = 131.58°. For guanidinium chlorodifluoroacetate and chlorodifluoroacetic acid, the 35Cl spin lattice relaxation time T1 and the line width have been followed up as a function of temperature. Therefrom, the activation energies of the reorientation motion of the group -CF2C1 have been determined to be 14 kJ • mol-1 (from T1) and 12.5 kJ • mol- 1 (from Δv) for the pure acid and 9.2 kJ • mol-1 and 8.8 kJ • mol-1 , respectively, for the guanidinium salt.

Machine Learning Models of Antibody–Excipient Preferential Interactions for Use in Computational Formulation Design

2020 ◽  
Vol 17 (9) ◽  
pp. 3589-3599 ◽  
Author(s):  
Theresa K. Cloutier ◽  
Chaitanya Sudrik ◽  
Neil Mody ◽  
Hasige A. Sathish ◽  
Bernhardt L. Trout
Keyword(s):  
Machine Learning ◽  
Learning Models ◽  
Formulation Design ◽  
Preferential Interactions ◽  
Machine Learning Models

scholarly journals Incorporation of Proteins with Different Isoelectric Points into Biomimetic Ca-P Coatings: A New Approach to Produce Hybrid Coatings with Tailored Properties

2006 ◽  
Vol 309-311 ◽  
pp. 755-758 ◽  
Author(s):  
H.S. Azevedo ◽  
Isabel B. Leonor ◽  
Rui L. Reis
Keyword(s):  
Calcium Phosphate ◽  
Bovine Serum Albumin ◽  
Hybrid Coating ◽  
Hybrid Coatings ◽  
New Approach ◽  
Phosphate Ions ◽  
Preferential Interactions ◽  
Isoelectric Points ◽  
Different Characteristics ◽  
Positively Charged

This work aims to study the effect of incorporating proteins with different isoelectric points (pI) on the structure, composition and morphology of biomimetic calcium-phosphate (Ca-P) coatings. For that, bovine serum albumin (BSA) and lysozyme, having respectively acidic and basic pIs, were used as model proteins. It was observed that the incorporation of positively charged proteins, such as lysozyme, was able to significantly change the structure of the coatings, possibly due to the preferential interactions between the protein and negatively charged phosphate ions. These results indicated that proteins with different characteristics can be incorporated into biomimetic Ca-P coatings in order to obtain a hybrid coating and at the same tailoring their properties.

The role of preferential interactions between similar domains in determining the behavior of aqueous solutions of aminoalkanols. A microcalorimetric study

1998 ◽  
Vol 313 (2) ◽  
pp. 125-130 ◽  
Author(s):  
Giuseppina Castronuovo ◽  
Vittorio Elia ◽  
M.Rosaria Tranchino ◽  
Filomena Velleca
Keyword(s):  
Aqueous Solutions ◽  
Preferential Interactions

scholarly journals Preferential Interactions of Fluorescent Probe Prodan with Cholesterol

1999 ◽  
Vol 76 (2) ◽  
pp. 956-962 ◽  
Author(s):  
Olga P. Bondar ◽  
Elizabeth S. Rowe
Keyword(s):  
Fluorescent Probe ◽  
Preferential Interactions
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