Tyrosine fluorescence probing of the surfactant-induced conformational changes of albumin

2015 ◽  
Vol 14 (5) ◽  
pp. 897-908 ◽  
Author(s):  
Nadezda G. Zhdanova ◽  
Evgeny A. Shirshin ◽  
Eugene G. Maksimov ◽  
Ivan M. Panchishin ◽  
Alexander M. Saletsky ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Native Proteins ◽  
Tyrosine Fluorescence ◽  
Fluorescence Probing

Tyrosine fluorescence in native proteins is known to be effectively quenched, whereas its emission increases upon proteins’ unfolding.

Tyrosine fluorescence probing of conformational changes in tryptophan-lacking domain of albumins

2017 ◽  
Vol 174 ◽  
pp. 223-229 ◽  
Author(s):  
N.G. Zhdanova ◽  
E.G. Maksimov ◽  
A.M. Arutyunyan ◽  
V.V. Fadeev ◽  
E.A. Shirshin
Keyword(s):  
Conformational Changes ◽  
Tyrosine Fluorescence ◽  
Fluorescence Probing

Substituting the Thiol Ester of Human A2M or C3 with a Disulfide Produces Native Proteins with Altered Proteolysis-Induced Conformational Changes

Biochemistry ◽  
2020 ◽  
Vol 59 (51) ◽  
pp. 4799-4809
Author(s):  
Seandean Lykke Harwood ◽  
Nadia Sukusu Nielsen ◽  
Henrik Pedersen ◽  
Katarzyna Kjøge ◽  
Peter Kresten Nielsen ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Thiol Ester ◽  
Native Proteins

scholarly journals The Improvement of Nanoemulsion Stability and Antioxidation via Protein-Chlorogenic Acid-Dextran Conjugates as Emulsifiers

Nanomaterials ◽  
2020 ◽  
Vol 10 (6) ◽  
pp. 1094 ◽  
Author(s):  
Chang Liu ◽  
Hua Jin ◽  
Yue Yu ◽  
Jingying Sun ◽  
Huanyu Zheng ◽  
...  
Keyword(s):  
Chlorogenic Acid ◽  
Conformational Changes ◽  
Soybean Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Isolate ◽  
Soybean Protein Isolate ◽  
Molecular Weights ◽  
Native Proteins ◽  
Fluorescence Measurements

In this experiment, the peanut protein isolate (PPI), soybean protein isolate (SPI), rice bran protein isolate (RBPI), and whey protein isolate (WPI) were modified by linking chlorogenic acid covalently and linking dextran by Maillard reaction to prepare protein-chlorogenic acid-dextran (PCD) conjugates. As for structures, conformational changes of conjugates were determined by Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE), Fourier transform infrared (FT-IR), and fluorescence measurements. The molecular weights of PCD conjugates became larger, the structure became disorder, and the amino acid residues inside the protein were exposed to the polar environment when compared to protein-chlorogenic acid (PC) and native proteins (NPs). As for properties, the interfacial tension reduced and antioxidant activity of PCD conjugates enhanced in varying degrees. Based on this, PCD conjugates were used as emulsifiers in order to investigate the properties of nanoemulsions and compared with PC conjugates and NPs. The mean droplet diameters (MDD) results showed that the nanoemulsions that were stabilized by PCD conjugates had the smallest particle sizes and exhibited uniformly dispersed spherical shapes. The storage and oxidative stabilities of PCD conjugates were also significantly improved. In comparison, nanoemulsion that was stabilized by PPI-chlorogenic acid-dextran conjugate had the smallest particle size and optimal stability among four protein stabilized nanoemulsions.

scholarly journals Conformational changes induced by binding of bivalent cations to oncomodulin, a paravalbumin-like tumour protein

1984 ◽  
Vol 220 (1) ◽  
pp. 261-268 ◽  
Author(s):  
J P MacManus ◽  
A G Szabo ◽  
R E Williams
Keyword(s):  
Conformational Change ◽  
Conformational Changes ◽  
The Other ◽  
Excitation Spectra ◽  
Fluorescence Excitation ◽  
Protein Protein Interaction ◽  
Tyrosine Fluorescence ◽  
Bivalent Cations ◽  
Fluorescence Excitation Spectra ◽  
Dependent Protein

When Mg2+ was added to rat oncomodulin, a paravalbumin-like tumour protein, changes in the c.d. spectrum and tyrosine fluorescence intensity were observed. The addition of Ca2+ resulted in even greater changes in these spectra. The fluorescence excitation spectra of apo- and Mg-oncomodulin were superimposable, whereas that of Ca-oncomodulin was markedly different. The u.v.-absorption spectrum of the Ca2+ form also showed major differences from those of the other two forms. These observations indicate that Ca2+ induced a significant and specific conformational change in the protein that was not observed on binding Mg2+. In contrast, the conformational change induced by either Mg2+ or Ca2+ was identical in the homologous rat parvalbumin. This Ca2+-specific conformational change may be the basis for oncomodulin's Ca2+-dependent protein/protein interaction.

scholarly journals Native proteins trap high-energy transit conformations

2015 ◽  
Vol 1 (9) ◽  
pp. e1501188 ◽  
Author(s):  
Andrew E. Brereton ◽  
P. Andrew Karplus
Keyword(s):  
Protein Folding ◽  
Conformational Changes ◽  
Protein Function ◽  
Protein Structures ◽  
High Energy ◽  
Native Proteins ◽  
Regulate Protein ◽  
The Right ◽  
And Function ◽  
Open Question

During protein folding and as part of some conformational changes that regulate protein function, the polypeptide chain must traverse high-energy barriers that separate the commonly adopted low-energy conformations. How distortions in peptide geometry allow these barrier-crossing transitions is a fundamental open question. One such important transition involves the movement of a non-glycine residue between the left side of the Ramachandran plot (that is, ϕ < 0°) and the right side (that is, ϕ > 0°). We report that high-energy conformations with ϕ ~ 0°, normally expected to occur only as fleeting transition states, are stably trapped in certain highly resolved native protein structures and that an analysis of these residues provides a detailed, experimentally derived map of the bond angle distortions taking place along the transition path. This unanticipated information lays to rest any uncertainty about whether such transitions are possible and how they occur, and in doing so lays a firm foundation for theoretical studies to better understand the transitions between basins that have been little studied but are integrally involved in protein folding and function. Also, the context of one such residue shows that even a designed highly stable protein can harbor substantial unfavorable interactions.

scholarly journals Conformation switching of single native proteins revealed by nanomechanical probing without a pulling force

Nanoscale ◽  
2019 ◽  
Vol 11 (42) ◽  
pp. 19933-19942
Author(s):  
Fabiola A. Gutiérrez-Mejía ◽  
Christian P. Moerland ◽  
Leo J. van IJzendoorn ◽  
Menno W. J. Prins
Keyword(s):  
Single Molecule ◽  
Conformational Changes ◽  
Biological Function ◽  
Single Molecule Level ◽  
Native Proteins ◽  
Protein Conformational Changes ◽  
P Protein ◽  
Heterogeneous Nature ◽  
Pulling Force

Protein conformational changes are essential to biological function, and the heterogeneous nature of the corresponding protein states provokes an interest to measure conformational changes at the single molecule level.

scholarly journals Real-Time Conformational Changes and Controlled Orientation of Native Proteins Inside a Protein Nanoreactor

2017 ◽  
Vol 139 (51) ◽  
pp. 18640-18646 ◽  
Author(s):  
Veerle Van Meervelt ◽  
Misha Soskine ◽  
Shubham Singh ◽  
Gea K. Schuurman-Wolters ◽  
Hein J. Wijma ◽  
...  
Keyword(s):  
Real Time ◽  
Conformational Changes ◽  
Native Proteins

scholarly journals Conformational changes in subdomain 2 of G-actin: fluorescence probing by dansyl ethylenediamine attached to Gln-41

1995 ◽  
Vol 69 (5) ◽  
pp. 2024-2032 ◽  
Author(s):  
E. Kim ◽  
M. Motoki ◽  
K. Seguro ◽  
A. Muhlrad ◽  
E. Reisler
Keyword(s):  
Conformational Changes ◽  
Fluorescence Probing

Influence of Calcium Ions on the Plant Cell Surface: Membrane Fusions and Conformational Changes

1974 ◽  
Vol 32 ◽  
pp. 154-155
Author(s):  
D. James Morré ◽  
Charles E. Bracker ◽  
William J. VanDerWoude
Keyword(s):  
Cell Wall ◽  
Cell Surface ◽  
Conformational Changes ◽  
Calcium Ions ◽  
Surface Membrane ◽  
Carboxyl Groups ◽  
Cross Linking ◽  
Ultrastructural Evidence ◽  
Glycine Max L ◽  
Wall Extensibility

Calcium ions in the concentration range 5-100 mM inhibit auxin-induced cell elongation and wall extensibility of plant stems. Inhibition of wall extensibility requires that the tissue be living; growth inhibition cannot be explained on the basis of cross-linking of carboxyl groups of cell wall uronides by calcium ions. In this study, ultrastructural evidence was sought for an interaction of calcium ions with some component other than the wall at the cell surface of soybean (Glycine max (L.) Merr.) hypocotyls.

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