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Research has been conducted on the hydrophobic core of ribonuclease T1. The use of the differential scanning calorimetry, urea denaturation and X-ray crystallography in investigating the structural and energetic results of the hydrophobic core's engineered cavity refilling with CH (sub)3, SH and OH groups is described.

Research has been conducted on the buried and well-ordered solvent molecules. The exchange kinetics of the water molecules with solvent has been examined.

Hydrogen-exchange rates for RNase T1 and variants with Ala results in Gly substitutions at a solvent-exposed position in the helix have been measured. Results demonstrate the change of the hydrogen-exchange stabilities of residues by Ala results in Gly mutations.

The protein kinase Akt is one of the primary effectors of growth factor signaling in the cell. Akt responds specifically to the lipid second messengers phosphatidylinositol-3,4,5-trisphosphate [PI(3,4,5)P3] and phosphatidylinositol-3,4-bisphosphate [PI(3,4)P2] via its PH domain, leading to phosphorylation of its activation loop and the hydrophobic motif of its kinase domain, which are critical for activity. We have now determined the crystal structure of Akt1, revealing an autoinhibitory interface between the PH and kinase domains that is often mutated in cancer and overgrowth disorders. This interface persists even after stoichiometric phosphorylation, thereby restricting maximum Akt activity to PI(3,4,5)P3- or PI(3,4)P2-containing membranes. Our work helps to resolve the roles of lipids and phosphorylation in the activation of Akt and has wide implications for the spatiotemporal control of Akt and potentially lipid-activated kinase signaling in general. [ABSTRACT FROM AUTHOR]

Many publications on dementia start by outlining the current estimated number of people with dementia and how that figure is going to double (in Western societies) or even quadruple (in developing countries) in the coming decades as a result of increasing life expectancy (in itself a good development). Dementia is therefore a huge challenge to society, both in terms of providing good care for persons living with dementia and their family caregivers, as well as in searching for curative solutions. Both these challenges are complex. Fortunately, recent research indicates primary prevention to be a promising additional strategy in the dementia quest. Now that epidemiological research robustly shows the link between lifestyle and risk of dementia, new challenges emerge, such as how to increase public awareness about brain health, how to develop and implement strategies to promote brain healthy lifestyles and how to avoid increasing health inequalities. Interdem, the pan-European network of researchers on Psychosocial Interventions in Dementia, strongly welcomes this new strategy and consequently established a taskforce on primary prevention. In this position paper, we outline what we see as main building blocks of primary prevention of dementia. [ABSTRACT FROM AUTHOR]

The use of information technology (IT) in human services has seen a very slow progress, and its introduction in schools of social work ha been evenslower. The quality and quantity of work by the social workers will ultimately suffer, as presentation of figures on their work may not be easily possible. This could lead to a decrease in funding for needed services. Not being able to get information about clients will hamper services that do exist. The increasing demand for efficiency and effectiveness calls for faster introduction of IT in social services.

Phosphodiester transesterification process involves the Glu58 which acts as a catalyst along with the RNase T1 enzyme. The Glu58 RNase T1 participates in the process by an altered mechanism where the Glu58 is replaced by His40 as a base catalyst. Guanine 2'-monophosphate is cocrystallized with Glu58Ala RNase T1 during the process. The structure of the Glu58 is obtained by the nominal resolution method.

The X-ray structure, gene structure and amino-acid arrangement of the orthorhombic crystal of the lentil lectin at 2.3-angstrom resolution are examined. Crystallography is used to study the high-resolution legume lectin structure. The geometrics of pea and lathyrus lectin are contrasted with that of the crystal. The binding of the carbohydrates and the activation of the posttranslation are affected by the structure. Hundred-and-eighty amino acids are included in the amino acid arrangement of the beta-chain. The temporary metal-binding site shows distinct variations in structure.