Structural characterization of recombinant bovine Go alpha by spectroscopy and homology modeling

Date

2011-01-01

Author

MEGA TİBER, PINAR
Orun, Oya
Nacar, Cevdet
Sezerman, Ugur Osman
Severcan, Feride
Severcan, Mete
Matagne, Andre
KAN, BEKİ

Metadata

Show full item record

This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Item Usage Stats

218
views

0
downloads

Go, a member of heterotrimeric guanine nucleotide-binding proteins, is the most abundant form of G protein in the central and peripheral nervous systems. Go alpha has a significant role in neuronal development and function but its signal transduction mechanism remains to be clarified.

Subject Keywords

Go alpha protein, Homology modeling, Circular dichroism, FTIR spectroscopy

URI

https://hdl.handle.net/11511/57547

Journal

SPECTROSCOPY-BIOMEDICAL APPLICATIONS

DOI

https://doi.org/10.3233/spe-2011-0543

Collections

Department of Biology, Article

Suggestions

OpenMETU
Core

Molecular docking study of fda-approved drugs to inhibit the bacterial ribosome Ateş, Beril; Yüce, Merve; Levitaş, Ozge Kurkcuoglu; Sungur, Fethiye Aylin (Orta Doğu Teknik Üniversitesi Enformatik Enstitüsü; 2022-10) Ribosomes are large macromolecular complexes responsible for cellular protein synthesis. It consists of two subunits; called 30S small and 50S large subunits in bacteria, involving antibiotic binding regions. This mac- romolecular machine is one of the significant targets of conventional antibiotics because protein synthesis can be stopped by targeting functional sites in the ribosome. For instance, several antibiotics target the decoding center responsible for deciphering the genetic code, as well as mRNA ...
INVESTIGATION OF PHYSICAL INTERACTION BETWEEN Gαi AND Gαs PROTEINS VIA FRET IN LIVE CELLS Balkan, Seyda Tuğçe; Son, Çağdaş Devrim; Küçük Baloğlu, Fatma; Department of Biochemistry (2021-8-11) GPCR’s are seven-transmembrane receptors that transmit external signals to the intracellular environment via secondary messenger systems through heterotrimeric G proteins. Heterotrimeric G proteins consist of α and β-γ subunits. Until recent years, scientists thought that GPCR signal transduction occurs between one GPCR and one heterotrimeric G protein; however, recently, it has been shown that GPCR’s can make oligomers. Oligomerization of GPCR allows cells to tune the intensity of the signal and respond ap...
Prediction of protein subcellular localization based on primary sequence data Özarar, Mert; Atalay, Mehmet Volkan; Department of Computer Engineering (2003) Subcellular localization is crucial for determining the functions of proteins. A system called prediction of protein subcellular localization (P2SL) that predicts the subcellular localization of proteins in eukaryotic organisms based on the amino acid content of primary sequences using amino acid order is designed. The approach for prediction is to nd the most frequent motifs for each protein in a given class based on clustering via self organizing maps and then to use these most frequent motifs as features...
Protein-Protein Interactions in Live Cells: Reinventing the Wheel Son, Çağdaş Devrim (2018-12-13) G protein-coupled receptors (GPCRs) are membrane proteins that mediate physiologicalresponse to a diverse array of stimuli. In humans, they mediate the action of hundreds ofpeptide hormones, sensory stimuli, odorants, neurotransmitters, and chemokines. GPCRs alsoare targets for ~40% of all currently marketed pharmaceuticals. These receptors traditionallybeen thought to act as monomeric units. However, recent evidence suggests that GPCRs mayform dimers as part of their normal trafficking and function. While ...
Molecular cloning, characterization, and expression analysis of a gene encoding a Ran binding protein (RanBP) in Cucumis melo L. Baloglu, Mehmet Cengiz; Zakharov, Florence Negre; Öktem, Hüseyin Avni; Yücel, Ayşe Meral (2011-01-01) Ran binding proteins (RanBPs) are highly conserved members of the GTP-binding protein family that are involved in nuclear protein export between the nucleus and the cytoplasm. In this study, a CmRanBP gene from a melon was isolated (Cucumis melo L.) using the RACE (rapid amplification of cDNA ends) method. The 778 basepair long melon, with a RanBP cDNA encoding consisting of 197 amino acids (22.2 kDa protein), was characterized (GenBank accession no: EU853459). The predicted amino acid sequence of CmRanBP w...

Citation Formats

P. MEGA TİBER et al., “Structural characterization of recombinant bovine Go alpha by spectroscopy and homology modeling,” SPECTROSCOPY-BIOMEDICAL APPLICATIONS, pp. 213–229, 2011, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/57547.