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.The adverse effects of a joint ROM restriction in elderly hip fracture patients.
Joint range of motion (ROM) restriction is a common therapy in elderly hip fracture patients. By reducing the ROM, the intensity and the extent of muscle activation and thereby increasing the oxygen cost of locomotion are reduced. We hypothesize that a ROM restriction will lead to a loss of muscle mass and strength in hip fracture patients. Additionally, the effort of locomotion required and the degree of self-care activities that can be performed will be reduced. To test our hypothesis, we determined the ROM in the hip and knee joints and the leg length difference in a group of 25 elderly inpatients with hip fractures. In addition, we assessed muscle power, muscle volume and performance of functional mobility activities. Our data show that restricting the hip and knee ROM led to a significantly decreased muscle strength, muscle power and lower performance of functional mobility activities. Compared with an age- and gender-matched group of healthy elderly, these patients were also impaired in muscle mass and muscle strength, especially the leg extensor muscles. These findings suggest that ROM restriction may have adverse effects on muscle mass and strength in older adults with hip fractures, affecting the ability to carry out daily activities.Structural and mechanistic determinants of alcohol dehydrogenase substrate specificity.
The enzyme Alcohol Dehydrogenase catalyzes the conversion of alcohols to the corresponding aldehydes in the presence of nicotinamide adenine dinucleotide (NAD(+)) in a reductive half-reaction that releases a reduced form of nicotinamide. The specificity of this enzymatic reaction is determined by substrate binding and subsequent conformational changes that are associated with the reduction of the nicotinamide cofactor, leading to the specific hydrogen bond interactions with the nicotinamide 2′-hydroxyl group. The primary specificity is determined by a binding site composed of the nicotinamide ring, which acts as a rigid scaffold onto which the substrate binds and interacts with residues from the catalytic site. A model of the interaction between the nicotinamide 2′-hydroxyl group and the catalytic residues in the active site has been developed by using molecular dynamics simulation. Our model accounts for the aromatic interaction of the nicotinamide ring with the tyrosine ligand and shows that steric interactions are the dominant driving forces. Similarities in the structure and shape of the active sites of other members of this enzyme family provide
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