Structural insights into protein quality control using cross linking mass spectrometry

2022-03-19
Özcan Kabasakal, Süreyya
Akkulak, Hatice
Göç, Günce
çalışseki, mehmet
İnce, H. Kerim
Lebrilla, Carlito B.
Berger-Schaffitzel, Christiane
KABASAKAL, BURAK VELİ
ACS Spring Meeting

Suggestions

Structural Insights into Alternate Aggregated Prion Protein Forms
POLANO, maurizio; Bek, Alpan; BENETTİ, federico; lazzarino, marco; LEGNAME, giuseppe (Elsevier BV, 2009-11-13)
The conversion of the cellular form of the prion protein (PrPC) to an abnormal, alternatively folded isoform (PrPSc) is the central event in prion diseases or transmissible spongiform encephalopathies. Recent studies have demonstrated de novo generation of murine prions from recombinant prion protein (recPrP) after inoculation into transgenic and wild-type mice. These so-called synthetic prions lead to novel prion diseases with unique neuropathological and biochemical features. Moreover, the use of recPrP i...
Structural modelling and functional analysis of the engineered small heat-shock protein, tpv-hsp14.3 from thermoplasma volcanium
Sheraj, Ilir; Kocabıyık, Semra; Department of Biology (2014)
In this study, a small heat shock protein tpv-Hsp14.3 from a thermoacidophilic Archaeon, Thermoplasma volcanium was studied. sHSPs are low molecular weight proteins involved in different stress responses to protect the cellular proteome and enhance survival of the host organism. For structure-function analysis of the protein, both experimental and computational tools were used. Sequence alignments with closely-related sHSPs showed high sequence conservation at the core α-Crystalline domain and a V/I/L-X-V/I...
STRUCTURAL MODIFICATIONS IN AN ARCHAEAL SMALL HEAT SHOCK PROTEIN TO REVEAL MOLECULAR BASIS OF SUBSTRATE TARGETING AND BINDING
Rafiq, Azra; Kocabıyık, Semra; Bat, Erhan; Department of Biochemistry (2022-5-12)
The N-terminal domain (NTD) of small heat shock protein (sHSP) from archaea, Thermoplasma volcanium, is highly hydrophobic in the proximal and distal end. It is 32 amino acids long and has two highly conserved glutamic acid residues at positions 11 and 22. The 3-D model of the dimer generated by homology modelling predicted the NTD to be running away from each other and the dimer interface being formed mainly between β2 and β6 sheets of the Alpha Crystallin Domain (ACD). The decrease in hydrophobicity in th...
Structural and functional investigation of the interaction of agomelatine with model membranes
Ergün, Seza; Severcan, Feride; Department of Biology (2012)
Depression is one of the most commonly seen psychiatric diseases in the population in recent years. Treatment of depression is mainly carried out by psychiatric drugs. In the past few years, agomelatine which is released to the market with a trade name, Valdoxane, has been thought to have far less side effects due to its non-addictive nature, not having trouble when the drug is quitted, and also due to its property of binding only to the specific receptor that the drug interacts with. The action mechanism o...
Structural investigation of donor age effect on human bone marrow mesenchymal stem cells: FTIR spectroscopy and imaging
Aksoy, Ceren; AERTS KAYA, FATİMA SUSANNA F.; KUŞKONMAZ, BÜLENT BARIŞ; Uckan, Duygu; Severcan, Feride (2014-08-01)
Stem cell studies hold enormous potential for development of new therapies for tissue regeneration and repair. Bone marrow mesenchymal stem cells (BM-MSCs) can differentiate into a variety of nonhematopoietic tissues and contribute maintenance of healthy hematopoiesis by providing supportive cellular microenvironment into BM. Here, we investigated age-related differences in BM-MSCs by using attenuated total reflection Fourier transform infrared (ATR-FTIR) spectroscopy and FTIR imaging together with hierarch...
Citation Formats
S. Özcan Kabasakal et al., “Structural insights into protein quality control using cross linking mass spectrometry,” presented at the ACS Spring Meeting, Amerika Birleşik Devletleri, 2022, Accessed: 00, 2022. [Online]. Available: https://hdl.handle.net/11511/99934.