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Application of a method of normal fashions for analysis of canals and pores


The method of normal fashions is successfully applied to studying of dynamic properties of pores and canals in squirrels. From protein VirE2 the method was not applied earlier to studying of properties of a possible pore.
However by means of the given method are considered dynamics and changes konformatsii many known porovyh complexes.
Gramitsidin And - the first membranous protein which has been investigated by a method of normal fashions [Roux, Karplus, 1988]. Dimernyj a complex of this protein - least of the known ion channels which everyone monomeasures represents a left-handed spiral from 16 amino acids. Two spirals possess the mechanism of selective permeability for small kationov (Cs +, K +) and water moleculas through a narrow lumen along an axis of spirals.
Potassium channels - tetramery in which transmembrane (TM) spirals form the central pore through which ions are tolerated. The majority of potassium channels have similar frame, despite considerable distinctions in sequence. All of them contain two TM spirals on everyone the monomeasures, bound by a field from 30 aminokislotnyh the residual, known as a P-loop. Work Kunga and co-authors of 2002 [Kong et al was one of the first works where the method of normal fashions has been applied to studying of the mechanism of discovering of a pore of a potassium channel., 2002]. Research has shown for the first time the co-ordinated gyral locomotions of all TM spirals.
More later research [Shrivastava, Bahar, 2006] of some potassium channels a method of normal fashions has shown, that they possess the same mode of opening-closing of pores. This mode of locomotion is counterrotation of two polovinok moleculas round a cylindrical axis of symmetry, and is similar on co-ordinated skruchenno-torsionnye locomotions of all TM spirals.
In work [Valadie et al., 2003] dynamic and konformatsionnye properties mehanochuvstvitelnogo canal MscL Escherichia coli have been studied by means of a method of normal fashions (drawing 1.13). Attempt to perceive was a research Main objective how these canals can be discovered and defines, what part of proteins can be involved in conformational changes. The conformational changes having features of behaviour, systems reflecting symmetry were observed. In first three fashions symmetric conformational changes, characteristic for the proteins forming canals were observed. Locomotions of first three fashions remind opening, diaphragm closing in the camera. The given portal mechanism combines an inclination and gyral locomotion of spirals along a canal axis. Such mechanism is the general process for the given phylum of canals, that is canals where the architecture of a pore is similar to a funnel. Other canals, such as a nucleotide dependent [Johnson, Zagotta, 2001] and potassium channels [Jiang et al., 2002], have transmembrane architecture close to frame MscL. They also test gyral locomotions, together with a break of the secondary structural elements bound to discovering of the canal.

Drawing 1.13 Vector representation of movements of Ca-atoms mehanoselektivnogo canal MscL (a lateral view and from above) [Valadie et al., 2003].


In work [Taly et al., 2005] by means of a method of normal fashions motility gomopentamernogo а7 a nicotinic receptor atsetilholina (nAChR) (drawing 1.14) has been investigated. nAChR getero-or gomopentamernyj the integrated membranous protein with axial pseudo-symmetry of a perpendicular membrane to a plane. Each subunit can be divided into three ranges: extracellular, transmembrane and
The endocellular.
Among the first 10 low-frequency fashions only the first fashion creates the structural organisation similar to the portal mechanism of canals: wide discovering of the canal of a pore is invoked by the co-ordinated symmetric turn of protein with inverse rotations top (extracellular) and inferior (transmembrane) ranges.
Considerable conformational changes are observed in each subunit. These global symmetric rotary locomotions pentamernogo an albuminous complex remind the portal mechanism of other multidimensional ion channels proved in experimental data, and thus, possibly, describes the portal mechanism of opening - of closing of a nicotinic receptor atsetilholina.

Drawing 1.14 Portal mechanism of opening-closing of the canal of a nicotinic receptor atsetilholina, observed in the first fashion by means of a method of normal fashions [Taly et al, 2005].

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A source: GUSEV Jury Sergeevich. FRAME And FUNCTIONS of PROTEIN VirE2 In TRANSMISSION otsdnk VEUKARIOTICHESSKY CAGES. 2014

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