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Biomedical subjects

A P Turnbull

Publications and source records attributed to A P Turnbull.

At least 19 recordsLinked to original sources
PubMed2005

Conceptualizing and measuring family quality of life.

BACKGROUND: Increasing emphasis on family-centred approaches to services and supports for families of children with disabilities has surfaced the issue of accountability for family outcomes. We present a review of literature about the impacts of children with disabilities on families as a backdrop to proposing family quality of life as a concept that encompasses impacts of disability and one that can be used to assess the impact of supports and services on families. METHOD: We briefly introduce the Beach Center Family Quality of Life Scale, providing information about its factor structure, reliability and convergent validity. RESULTS: The Beach Center Family Quality of Life Scale contains 25 items assessing family ratings of importance and satisfaction with five domains: Family interaction, Parenting, Emotional well-being, Physical/material well-being and Disability-related supports. CONCLUSION: We present a framework for utilizing a measure of family quality of life as a long-term outcome in concert with other short-term measures of service outcomes for families.

Family↗
PubMed2002

Crystallization and preliminary X-ray analysis of the ytxM gene product from Bacillus subtilis.

The ytxM gene product from Bacillus subtilis has been cloned, expressed in Escherichia coli, purified and crystallized by the hanging-drop vapour-diffusion method using PEG 3350 as the precipitant. Multiple-wavelength anomalous dispersive X-ray data have been collected to 2.0 A resolution on a single selenomethionine-incorporated crystal. This crystal belongs to the primitive orthorhombic system, with approximate unit-cell parameters a = 44.3, b = 90.9, c = 136.1 A, alpha = beta = gamma = 90 degrees and two monomers in the asymmetric unit.

Amino Acid Sequence↗
PubMed2001

Analysis of the structure, substrate specificity, and mechanism of squash glycerol-3-phosphate (1)-acyltransferase.

BACKGROUND: Glycerol-3-phosphate (1)-acyltransferase(G3PAT) catalyzes the incorporation of an acyl group from either acyl-acyl carrier proteins (acylACPs) or acyl-CoAs into the sn-1 position of glycerol 3-phosphate to yield 1-acylglycerol-3-phosphate. G3PATs can either be selective, preferentially using the unsaturated fatty acid, oleate (C18:1), as the acyl donor, or nonselective, using either oleate or the saturated fatty acid, palmitate (C16:0), at comparable rates. The differential substrate specificity for saturated versus unsaturated fatty acids seen within this enzyme family has been implicated in the sensitivity of plants to chilling temperatures. RESULTS: The three-dimensional structure of recombinant G3PAT from squash chloroplast has been determined to 1.9 A resolution by X-ray crystallography using the technique of multiple isomorphous replacement and provides the first representative structure of an enzyme of this class. CONCLUSIONS: The tertiary structure of G3PAT comprises two domains, the larger of which, domain II, features an extensive cleft lined by hydrophobic residues and contains at one end a cluster of positively charged residues flanked by a H(X)(4)D motif, which is conserved amongst many glycerolipid acyltransferases. We predict that these hydrophobic and positively charged residues represent the binding sites for the fatty acyl substrate and the phosphate moiety of the glycerol 3-phosphate, respectively, and that the H(X)(4)D motif is a critical component of the enzyme's catalytic machinery.

Amino Acid Sequence↗
PubMed2001

Crystallization and preliminary X-ray analysis of the glycerol-3-phosphate 1-acyltransferase from squash (Cucurbita moschata).

Glycerol-3-phosphate 1-acyltransferase (E.C. 2.3.1.15; G3PAT) catalyses the incorporation of an acyl group from either acyl-acyl carrier proteins (acylACPs) or acylCoAs into the sn-1 position of glycerol 3-phosphate to yield 1-acylglycerol 3-phosphate. Crystals of squash G3PAT have been obtained by the hanging-drop method of vapour diffusion using PEG 4000 as the precipitant. These crystals are most likely to belong to space group P2(1)2(1)2(1), with approximate unit-cell parameters a = 61.1, b = 65.1, c = 103.3 A, alpha = beta = gamma = 90 degrees and a monomer in the asymmetric unit. X-ray diffraction data to 1.9 A resolution have been collected in-house using a MAR 345 imaging-plate system.

Acyltransferases↗
PubMed2001

Perspectives of dentists, families, and case managers on dental care for individuals with developmental disabilities in Kansas.

The status of dental care for individuals with developmental disabilities in Kansas was examined. Dentists, family members, and case managers reported general, but partial, satisfaction with the availability, accessibility, appropriateness, and affordability of such care. Reasons for the results and recommendations for further improvement are discussed.

Adolescent↗
PubMed2000

Successful friendships of Hispanic children and youth with disabilities: an exploratory study.

Interviews were conducted with Hispanic children who had a disability and a friend with whom they had a successful friendship, as well as with parents and teachers. We focused the interviews on the children's and adults' descriptions of the friendship, what each of the children gave to and received from the friendship, the evolution of the friendship in terms of intensity, and the influence of Hispanic cultural values. A friendship support conceptual framework is presented to organize the data related to three relationship domains (companionship, instrumental support, and emotional support) and three friendship depth levels (acquaintance, casual, and intimate). We focused our key recommendations on future directions for research and friendship facilitation.

Adolescent↗
PubMed2000

Group action planning as a support strategy for Hispanic families: parent and professional perspectives.

Focus group interviews were conducted to obtain participants' preliminary reactions to the responsiveness of group action planning, a person-centered planning approach, as a support strategy for Hispanic families of individuals with disabilities. Focus group participants were 38 Hispanic parents of youth/young adults with developmental disabilities and 22 professionals who provided support services to Hispanic youth/young adults with developmental disabilities and their families. Both constituency groups identified advantages and disadvantages of group action planning. We focus our key recommendations on the implications of this information for education and human service systems as well as directions for future research.

Adolescent↗
PubMed2000

Mutagenesis of squash (Cucurbita moschata) glycerol-3-phosphate acyltransferase (GPAT) to produce an enzyme with altered substrate selectivity.

In an attempt to rationalize the relationship between structure and substrate selectivity of glycerol-3-phosphate acyltransferase (GPAT, 1AT, EC 2.3.1.15) we have cloned a number of cDNAs into the pET overexpression system using a PCR-based approach. Following assay of the recombinant enzyme we noted that the substrate selectivity of the squash (Cucurbita moschata) enzyme had altered dramatically. This form of GPAT has now been crystallized and its full three-dimensional structure elucidated. Since we now have two forms of the enzyme that display different substrate selectivities this should provide a powerful tool to determine the basis of the selectivity changes. Kinetic and structural analyses are currently being performed to rationalize the changes which have taken place.

Arabidopsis↗
PubMed1997

Determinants of substrate specificity in the superfamily of amino acid dehydrogenases.

The subunit of the enzyme glutamate dehydrogenase comprises two domains separated by a cleft harboring the active site. One domain is responsible for dinucleotide binding and the other carries the majority of residues which bind the substrate. During the catalytic cycle a large movement between the two domains occurs, closing the cleft and bringing the C4 of the nicotinamide ring and the Calpha of the substrate into the correct positioning for hydride transfer. In the active site, two residues, K89 and S380, make interactions with the gamma-carboxyl group of the glutamate substrate. In leucine dehydrogenase, an enzyme belonging to the same superfamily, the equivalent residues are L40 and V294, which create a more hydrophobic specificity pocket and provide an explanation for their differential substrate specificity. In an attempt to change the substrate specificity of glutamate dehydrogenase toward that of leucine dehydrogenase, a double mutant, K89L,S380V, of glutamate dehydrogenase has been constructed. Far from having a high specificity for leucine, this mutant appears to be devoid of any catalytic activity over a wide range of substrates tested. Determination of the three-dimensional structure of the mutant enzyme has shown that the loss of function is related to a disordering of residues linking the enzyme's two domains, probably arising from a steric clash between the valine side chain, introduced at position 380 in the mutant, and a conserved threonine residue, T193. In leucine dehydrogenase the steric clash between the equivalent valine and threonine side chains (V294, T134) does not occur owing to shifts of the main chain to which these side chains are attached. Thus, the differential substrate specificity seen in the amino acid dehydrogenase superfamily arises from both the introduction of simple point mutations and the fine tuning of the active site pocket defined by small but significant main chain rearrangements.

Amino Acid Oxidoreductases↗
PubMed1997

Analysis of the quaternary structure, substrate specificity, and catalytic mechanism of valine dehydrogenase.

The solution of the three-dimensional structure of Bacillus sphaericus leucine dehydrogenase has enabled us to undertake a homology-based modeling exercise on the sequence differences between the families of leucine (LeuDH) and valine (ValDH) dehydrogenases. This analysis indicates that the secondary structure elements in the core of the two domains of a single subunit of these enzymes are conserved, as are residues directly implicated in the recognition of the nucleotide cofactor and in catalysis. Comparison of the sequences indicates that the residues in the pocket accommodating the side chain of the amino acid substrate are conserved between these two enzymes, suggesting that the small differences in specificity arise from minor changes in molecular structure, possibly associated with shifts of the main chain rather than mutation of residues in the pocket itself. While B. sphaericus LeuDH is an octamer, both Streptomyces cinnamonensis and Streptomyces coelicolor ValDHs are dimers. The differences in quaternary structure can be understood in terms of the deletion in the latter of a C-terminal loop, which forms important interactions around the four-fold axis in LeuDH.

Amino Acid Oxidoreductases↗
PubMed1996

Family perspectives on problem behavior.

Data from interviews with 17 families who have a member with mental retardation and problem behavior were reported. The interview was focused on the families' definition of problem behavior, current challenges they face, and successful approaches for helping individuals with problem behavior and their families as well as suggestions from families about what kinds of information they believe would help them in addressing challenges. Key recommendations focus on the implications of this information for research, demonstration, and training activities.

Adolescent↗
PubMed1995

A role for quaternary structure in the substrate specificity of leucine dehydrogenase.

BACKGROUND: Glutamate, phenylalanine and leucine dehydrogenases catalyze the NAD(P)(+)-linked oxidative deamination of L-amino acids to the corresponding 2-oxoacids, and sequence homology between these enzymes clearly indicates the existence of an enzyme superfamily related by divergent evolution. We have undertaken structural studies on a number of members of this family in order to investigate the molecular basis of their differential amino acid specificity. RESULTS: We have solved the X-ray structure of the leucine dehydrogenase from Bacillus sphaericus to a resolution of 2.2 A. Each subunit of this octameric enzyme contains 364 amino acids and folds into two domains, separated by a deep cleft. The nicotinamide ring of the NAD+ cofactor binds deep in this cleft, which is thought to close during the hydride transfer step of the catalytic cycle. CONCLUSIONS: Comparison of the structure of leucine dehydrogenase with a hexameric glutamate dehydrogenase has shown that these two enzymes share a related fold and possess a similar catalytic chemistry. A mechanism for the basis of the differential amino acid specificity between these enzymes involves point mutations in the amino acid side-chain specificity pocket and subtle changes in the shape of this pocket caused by the differences in quaternary structure.

Amino Acid Oxidoreductases↗
PubMed1994

Crystallization and quaternary structure analysis of the NAD(+)-dependent leucine dehydrogenase from Bacillus sphaericus.

The NAD(+)-dependent leucine dehydrogenase from Bacillus sphaericus has been crystallized by the hanging drop method of vapour diffusion, using ammonium sulphate as the precipitant. The crystals belong to the tetragonal system and are in space group I4, with unit cell dimensions of a = b = 138.4 A and c = 121.8 A. Considerations of the values of Vm, the space group symmetry and an analysis of a self-rotation function calculated on a preliminary data set collected to 3 A resolution show that the asymmetric unit contains a dimer with the twofold axis perpendicular to the crystallographic four fold, indicating that the quaternary structure of this enzyme is octameric. Leucine dehydrogenase belongs to a superfamily of amino acid dehydrogenases which display considerable differences in amino acid specificity and elucidation of its three-dimensional structure should enable the molecular basis of this differential specificity to be examined in detail.

Amino Acid Oxidoreductases↗
PubMed1985

Developing independence.

The transition from living a life as others want (dependence) to living it as the adolescent wants to live it (independence) is extraordinarily difficult for most teen-agers and their families. The difficulty is compounded in the case of adolescents with disabilities. They are often denied access to the same opportunities of life that are accessible to the nondisabled. They face special problems in augmenting their inherent capacities so that they can take fuller advantage of the accommodations that society makes in an effort to grant them access. In particular, they need training designed to increase their capacities to make, communicate, implement, and evaluate their own life-choices. The recommendations made in this paper are grounded in the long-standing tradition of parens patriae and enlightened paternalism; they seek to be deliberately and cautiously careful about the lives of adolescents with disabilities and their families. We based them on the recent tradition of anti-institutionalism and they are also consistent with some of the major policy directions of the past 15-20 years. These include: normalization, integration, and least-restrictive alternatives; the unity and integrity of the family; the importance of opportunities for self-advocacy; the role of consumer consent and choice in consumer-professional relationships; the need for individualized services; the importance of the developmental model as a basis for service delivery; the value of economic productivity of people with disabilities; and the rights of habilitation, amelioration, and prevention.

Activities of Daily Living↗