Search results for "QUATERNARY STRUCTURE"
showing 10 items of 47 documents
Protein data condensation for effective quaternary structure classification
2007
Many proteins are composed of two or more subunits, each associated with different polypeptide chains. The number and the arrangement of subunits forming a protein are referred to as quaternary structure. The quaternary structure of a protein is important, since it characterizes the biological function of the protein when it is involved in specific biological processes. Unfortunately, quaternary structures are not trivially deducible from protein amino acid sequences. In this work, we propose a protein quaternary structure classification method exploiting the functional domain composition of proteins. It is based on a nearest neighbor condensation technique in order to reduce both the porti…
The Allosteric Effector l-Lactate Induces a Conformational Change of 2×6-meric Lobster Hemocyanin in the Oxy State as Revealed by Small Angle X-ray S…
2001
Abstract Hemocyanins are multisubunit respiratory proteins found in many invertebrates. They bind oxygen highly cooperatively. However, not much is known about the structural basis of this behavior. We studied the influence of the physiological allosteric effectorl-lactate on the oxygenated quaternary structure of the 2×6-meric hemocyanin from the lobster Homarus americanus employing small angle x-ray scattering (SAXS). The presence of 20 mm l-lactate resulted in different scattering curves compared with those obtained in the absence of l-lactate. The distance distribution functionsp(r) indicated a more compact molecule in presence ofl-lactate, which is also reflected in a reduction of the …
Quaternary structure and molecular model of a 4x6mer arthropod hemocyanin in oxygenated and deoxygenated states by 3D cryo-electron microscopy
2007
Extended abstract of a paper presented at MC 2007, 33rd DGE Conference in Saarbrücken, Germany, September 2 – September 7, 2007
Quaternary transition pathway in sol–gel encapsulated haemoglobin tracked by NIR and UV spectral relaxations
2008
→T structural transition of haemoglobin (hb), the protein responsible for oxygen (o) transport in the red blood cells of vertebrates, is the hall mark example. This transition, which regu lates o2 uptake in the lungs and o2 release in the tissues, is a switch in the quaternary structure of the protein from a low-affinity state (T) to a high-affinity state (R), two well-characterised structures. The struc tural pathway connecting the end states of this transition remains unclear, however, although recently several experimental 1 or
The SARS-CoV-2 envelope (E) protein has evolved towards membrane topology robustness.
2021
- Single-spanning SARS-CoV-2 envelope (E) protein topology is a major determinant of protein quaternary structure and function. - Charged residues distribution in E protein sequences from highly pathogenic human coronaviruses (i.e., SARS-CoV, MERS-CoV and SARS-CoV-2) stabilize Ntout-Ctin membrane topology. - E protein sequence could have evolved to ensure a more robust membrane topology from MERS-CoV to SARS-CoV and SARS-CoV-2.
Spectroscopic markers of the T-R quaternary transition in human hemoglobin
2004
n questo lavoro, usiamo un protocollo sol-gel per intrappolare e confrontare gli stati quaternari R e T di entrambi i deossigenati (deossiHb) ederivati di ossido di carbonio (HbCO) dell'emoglobina umana. La banda di assorbimento ottico del vicino infrarosso III e lo stretching di CO a infrarossibanda sono utilizzati per rilevare l'effetto della struttura quaternaria sulle proprietà spettrali di deoxyHb e HbCO; confronto con mioglobinaconsente una valutazione dei contributi terziari e quaternari ai turni di banda misurati. La RXLa transizione T è indicata per causare un bluspostamento della banda III di ~ 35 cm?1per deoxyHb e uno spostamento rosso della banda di allungamento CO di soli ~ 0…
Small angle neutron scattering study of the quaternary structure of haemocyanin of Rapana thomasiana
1996
Abstract Small angle neutron scattering (SANS) experiments were performed on a series of solutions of haemocyanin (Hc) of Rapana thomasiana . In a first series of solutions, by changing the external contrast a model of the molecule that is apparently in disagreement with electron microscopy (EM) measurements was obtained. The apparent disagreement was resolved by performing experiments on a series of variable protein concentration solutions in D 2 O. The physical parameters of the model, extrapolated to zero concentration, are in excellent agreement with the EM results obtained on samples more dilute than those examined with SANS.
Quaternary and subunit structure of Calliphora arylphorin as deduced from electron microscopy, electrophoresis, and sequence similarities with arthro…
1992
Arylphorin was purified from larvae of the blowfly Calliphora vicina and studied in its oligomeric form and after dissociation at pH 9.6 into native subunits. In accordance with earlier literature, it was electrophoretically shown to be a 500 kDa hexamer (1 x 6) consisting of 78 kDa polypeptides (= subunits). Electron micrographs of negatively stained hexamers show a characteristic curvilinear, equilateral triangle of 12 nm in diameter (top view) and a rectangle measuring 10 x 12 nm (side view). Alternatively, particles in the top view orientation exhibit a roughly circular shape 12 nm in diameter. Crossed immunoelectrophoresis revealed the presence of a major subunit type; the nature of a …
Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering
2008
We demonstrate tracking of protein structural changes with time-resolved wide-angle X-ray scattering (TR-WAXS) with nanosecond time resolution. We investigated the tertiary and quaternary conformational changes of human hemoglobin under nearly physiological conditions triggered by laser-induced ligand photolysis. We also report data on optically induced tertiary relaxations of myoglobin and refolding of cytochrome c to illustrate the wide applicability of the technique. By providing insights into the structural dynamics of proteins functioning in their natural environment, TR-WAXS complements and extends results obtained with time-resolved optical spectroscopy and X-ray crystallography.
Introduction of histidine residues into avidin subunit interfaces allows pH-dependent regulation of quaternary structure and biotin binding
2003
AbstractIn order to turn the subunit association and biotin binding of avidin into pH-sensitive phenomena, we have replaced individually three amino acid residues in avidin (Met96, Val115 and Ile117) with histidines in the 1–3 interface, and in combination with a histidine conversion in the 1–2 interface (Trp110). The single replacements Met96His and Val115His in the 1–3 interface were found to have a clear effect on the quaternary structure of avidin, since subunit associations of these mutants became pH-dependent. The histidine replacement in the 1–2 interface affected the biotin-binding properties of the mutants, in particular reversibility of binding and protein–ligand complex formation…