An Academic-Practice Partnership: Fostering Collaboration and Improving Care Across Settings.

Background: Through the Veterans Affairs Nursing Academic Partnership (VANAP), baccalaureate nursing students and faculty participated in practice innovations in a Veterans Affairs Health Care System. Nationally, VANAP has attempted to bridge gaps between theory and practice and across care settings.

Approach: In a population health course, nursing students were placed in both inpatient and outpatient settings.

A Ca(2+)-binding chimera of human lysozyme and bovine alpha-lactalbumin that can form a molten globule.

In contrast to lysozymes, which undergo two-state thermal denaturation, the Ca(2+)-free form of the homologous alpha-lactalbumins forms an intermediate "molten globule" state. To understand this difference, we have produced a chimera of human lysozyme and bovine alpha-lactalbumin. In the synthetic gene of the former the sequence coding for amino acid residues 76-102 was replaced by that for bovine alpha-lactalbumin 72-97, which represents the Ca(2+)-binding loop and the central helix C.

An equilibrium partially folded state of human lysozyme at low pH.

Temperature-induced unfolding of human lysozyme has been monitored by circular dichroism and by nuclear magnetic resonance experiments at a variety of low pH values. The results indicate that, although at pH values above 3 unfolding appears to be consistent with a two-state model, at lower pH values this is not the case. At pH 1.

The refolding of human lysozyme: a comparison with the structurally homologous hen lysozyme.

Pulsed hydrogen exchange labeling has been used in conjunction with circular dichroism in the near and far UV to study the refolding of human lysozyme from its guanidinium chloride denatured state. Human lysozyme differs in sequence by 51 residues and one insertion from the hen protein, which has previously been studied under identical conditions by similar methods [Radford, S. E.