1 angstrom resolution The high-resolution refinement of the stru

1 angstrom resolution. The high-resolution refinement of the structure of R96H does not support the bond angle distortion seen in the 1.9 A structure determination. At the same learn more time, it does confirm other manifestations of strain seen previously including an unusual rotameric state for His96 with distorted hydrogen bonding. The rotamer strain has been estimated as about 0.8 kcal/mol, which is about 25% of the overall reduction in stability of

the mutant. Because of concern that contacts from a neighboring molecule in the crystal might influence the geometry at the site of mutation we also constructed and analyzed supplemental mutant structures in which this crystal contact was eliminated. High-resolution refinement shows that the crystal contacts have essentially no effect on the conformation of Arg96 in WT or on His96 in the R96H mutant.”
“Brain amyloid can be measured using positron emission tomography (PET). There are mixed reports regarding whether amyloid measures are correlated with measures of cognition (in particular memory), depending on the cohorts and cognitive domains assessed. In Alzheimer’s disease (AD) patients and those at heightened risk for AD, cognitive performance may be related to the level and extent of classical AD pathology (amyloid see more plaques and neurofibrillary angles), but it is also influenced by neurodegeneration,

neurocognitive reserve, and vascular health.

We discuss what recent neuroimaging research has discovered about cognitive deficits in AD and offer suggestions for future research.”
“To try to resolve the loss of stability in the temperature-sensitive mutant of T4 lysozyme, Arg 96 -> His, all of the remaining 18 naturally occurring amino acids were substituted at site 96. Also, in response to suggestions that the charged residues Lys85 and Asp89, which are 5-8 angstrom away, may have important effects, each of these amino acids was replaced with alanine. Crystal structures were determined for many of the variants. With the exception of the tryptophan and valine gmelinol mutants R96W and R96V, the crystallographic analysis shows that the substituted side chain following the path of Arg96 in wildtype (WT). The melting temperatures of the variants decrease by up to similar to 16 degrees C with WT being most stable. There are two site 96 replacements, with lysine or glutamine, that leave the stability close to that of WT. The only element that the side chains of these residues have in common with the WT arginine is the set of three carbon atoms at the C(alpha), C(beta), and C(gamma) positions. Although each side chain is long and flexible with a polar group at the distal position, the details of the hydrogen bonding to the rest of the protein differ in each case. Also, the glutamine replacement lacks a positive charge.

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