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Pregled bibliografske jedinice broj: 1149659

Protein self-association


Dončević, Lucija; Brkić, Antun Lovro; Cindrić, Mario
Protein self-association // XIV Christmas Biophysics Workshops Book of abstracts / Micheletti, Cristian ; Adroher-Benítez, Irene (ur.).
Trst: Scuola Internazionale Superiore di Studi Avanzati, 2019. str. 16-16 (predavanje, međunarodna recenzija, sažetak, ostalo)


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Naslov
Protein self-association

Autori
Dončević, Lucija ; Brkić, Antun Lovro ; Cindrić, Mario

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, ostalo

Izvornik
XIV Christmas Biophysics Workshops Book of abstracts / Micheletti, Cristian ; Adroher-Benítez, Irene - Trst : Scuola Internazionale Superiore di Studi Avanzati, 2019, 16-16

Skup
XIV Christmas Biophysics Workshops

Mjesto i datum
Gradisca d'Isonzo, Italija, 09-10.12.2019

Vrsta sudjelovanja
Predavanje

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
protein aggregates ; agitation ; rHuG-CSF ; filgrastim

Sažetak
Monomeric protein structure can form dimers, trimers and other aggregates induced by different types of stressors. During protein association process different types of bonding may occur, such as covalent, especially disulfide bonds, and non- covalent bonds: hydrogen bonds, electrostatic interactions, Van der Waals interactions and hydrophobic bonds. Protein structure complexity makes mechanism of aggregates emergence entirely unrevealed or poorly described. Affected by these stressors, covalent and non- covalent bondage may occur and produce irreversible or reversible protein aggregates. Irreversible aggregates can be produced through heating, freezing-thawing, over- concentrating, isomerization, oxidation, etc. On the other hand, reversible aggregates or self- associates might be formed by the aforementioned processes but most likely by agitation.1 We examined the formation of dimers, trimers, and tetramers on rHuG-CSG, also known as Granulocyte Colony Stimulating Factor, induced by agitation through a time period of 150 s. The analysis was performed immediately after agitation by liquid chromatography (gel permeation) at pH= 7.0 (50 mM NH4HCO3 mobile phase). Due to increased pressure caused by centripetal acceleration during agitation monomeric structures merges and makes dimers, trimers, tetramers, and other aggregates. Increased agitation power results in a significant increase of reversible self-associate quantity.

Izvorni jezik
Engleski

Znanstvena područja
Fizika, Kemija



POVEZANOST RADA


Ustanove:
Institut "Ruđer Bošković", Zagreb

Profili:

Avatar Url Antun Brkic (autor)

Avatar Url Mario Cindrić (autor)

Avatar Url Lucija Dončević (autor)

Poveznice na cjeloviti tekst rada:

people.sissa.it

Citiraj ovu publikaciju:

Dončević, Lucija; Brkić, Antun Lovro; Cindrić, Mario
Protein self-association // XIV Christmas Biophysics Workshops Book of abstracts / Micheletti, Cristian ; Adroher-Benítez, Irene (ur.).
Trst: Scuola Internazionale Superiore di Studi Avanzati, 2019. str. 16-16 (predavanje, međunarodna recenzija, sažetak, ostalo)
Dončević, L., Brkić, A. & Cindrić, M. (2019) Protein self-association. U: Micheletti, C. & Adroher-Benítez, I. (ur.)XIV Christmas Biophysics Workshops Book of abstracts.
@article{article, author = {Don\v{c}evi\'{c}, Lucija and Brki\'{c}, Antun Lovro and Cindri\'{c}, Mario}, year = {2019}, pages = {16-16}, keywords = {protein aggregates, agitation, rHuG-CSF, filgrastim}, title = {Protein self-association}, keyword = {protein aggregates, agitation, rHuG-CSF, filgrastim}, publisher = {Scuola Internazionale Superiore di Studi Avanzati}, publisherplace = {Gradisca d'Isonzo, Italija} }
@article{article, author = {Don\v{c}evi\'{c}, Lucija and Brki\'{c}, Antun Lovro and Cindri\'{c}, Mario}, year = {2019}, pages = {16-16}, keywords = {protein aggregates, agitation, rHuG-CSF, filgrastim}, title = {Protein self-association}, keyword = {protein aggregates, agitation, rHuG-CSF, filgrastim}, publisher = {Scuola Internazionale Superiore di Studi Avanzati}, publisherplace = {Gradisca d'Isonzo, Italija} }




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