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Facilitated positional release region

Facilitated positional release involves positioning a region or joint into neutral, luiloading the joint, adding a facihtating force (compression and/or torsion), adding motion in all three planes of freedom, and monitoring for release. The time interval is a few seconds. [Pg.99]

All facilitated positional release techniques for treating cervical region dysfunctions are begun with a slight flattening of the cervical lordosis. [Pg.150]

FIG. 29-1 Facilitated positional release treatment of superficial muscle hypertonicity of cervical region application of axial compression. [Pg.150]

FIQ. 29-2 Facilitated positional release treatment of muscle hypertonioity in the oen/ical region with extension and right side-bending added. [Pg.151]

Facilitated Positional Release in the thoracic region may be performed with the patient in either a seated position or in a prone position. If the patient is treated in a prone position, use of a pillow will be necessary. The pillow is placed under the patient s abdomen or head and neck to assist in flattening the thoracic kyphosis. [Pg.205]

Fig. 2. NAPI facilitates H2A, H2B release from nucleosomes that are on positively coiled DNA (A) but not negatively coiled DNA (B). The positively coiled DNA (6.0 kb) with a superhelical density of + 0.05 and negatively coiled DNA (6.0 kb) with a superhelical density of -0.05 were reconstituted with lysine, arginine-labeled histones H3, H4, H2A, H2B by NaCl dialysis from 2.0 M to 1.2 M to 0.6 M to 0.1 M NaCl over a 14 h period. The samples were incubated with NAPI at 35 °C for 5 min and applied to a 5-20% sucrose/100 mM NaCl/40 mM Tris, pH 7.8 gradient. After sedimentation at 200,000 X g for 5 h, fractions were collected and the distribution of DNA (bottom panel) was determined on agarose gel and the distribution of protein (top panel) on SDS-PAGE followed by fluorography. These data are unpublished observations (V. Levchenko and V. Jackson). The deg-H2A is degraded H2A in which a 15 amino acid peptide of the C terminal has been proteolytically removed. When H2A, H2B is no longer present in a nucleosome, the C terminal region is sensitive to proteolysis [126] from a protease which is a minor contaminate in the NAPI preparation. Fig. 2. NAPI facilitates H2A, H2B release from nucleosomes that are on positively coiled DNA (A) but not negatively coiled DNA (B). The positively coiled DNA (6.0 kb) with a superhelical density of + 0.05 and negatively coiled DNA (6.0 kb) with a superhelical density of -0.05 were reconstituted with lysine, arginine-labeled histones H3, H4, H2A, H2B by NaCl dialysis from 2.0 M to 1.2 M to 0.6 M to 0.1 M NaCl over a 14 h period. The samples were incubated with NAPI at 35 °C for 5 min and applied to a 5-20% sucrose/100 mM NaCl/40 mM Tris, pH 7.8 gradient. After sedimentation at 200,000 X g for 5 h, fractions were collected and the distribution of DNA (bottom panel) was determined on agarose gel and the distribution of protein (top panel) on SDS-PAGE followed by fluorography. These data are unpublished observations (V. Levchenko and V. Jackson). The deg-H2A is degraded H2A in which a 15 amino acid peptide of the C terminal has been proteolytically removed. When H2A, H2B is no longer present in a nucleosome, the C terminal region is sensitive to proteolysis [126] from a protease which is a minor contaminate in the NAPI preparation.
HsO ) in one region of an aqueous solution to produce a hydronium ion at a distant site. Note that the proton released locally from the initial HsO remains in its vicinity, and is not the same as the proton forming the hydronium ion at the distant site. For this reason, the ionic mobility appears to be much greater than would be expected on the basis of diffusion alone. Facilitated proton transfer along rigidly and accurately positioned hydrogen bonds could be of fundamental importance in enzyme catalysis. See Water... [Pg.326]


See other pages where Facilitated positional release region is mentioned: [Pg.277]    [Pg.650]    [Pg.308]    [Pg.236]    [Pg.611]    [Pg.487]    [Pg.881]    [Pg.180]    [Pg.111]    [Pg.104]    [Pg.612]    [Pg.881]    [Pg.80]    [Pg.467]    [Pg.311]    [Pg.148]    [Pg.422]    [Pg.237]    [Pg.115]    [Pg.219]    [Pg.85]    [Pg.3339]    [Pg.36]    [Pg.332]   
See also in sourсe #XX -- [ Pg.442 , Pg.443 ]




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