Pension accounting information and firm value: An analysis of FTSE 100 companies.

This study is among the first to take known results in pension accounting and use a sample of UK listed FTSE 100 companies to show that the results are mostly the same as in previous research (on the US companies) into associations between pension accounting information and firm value. We investigate the association between published pension accounting information and the market value of a sample of UK listed FTSE 100 companies in the ten-year period 2006 to 2015. We analyse UK listed firms that report under the IFRS accounting framework (IAS 19), which is a contribution to earlier literature that concentrated on US listed firms that report under the US (FASB) accounting framework that has significantly different pension accounting rules to the IFRS accounting framework.

Effect of deamidation on stability for the collagen to gelatin transition.

Deamidation of amide residues, Asn and Gln, in collagen occurs during the manufacture of B-type gelatin and could affect the performance of B-type gelatins as it may affect the refolding of triple-helical junctional domains that are formed during gelation. Host-guest peptides of the form acetyl-(Gly-Pro-Hyp)3-Gly-Xaa-Yaa-(Gly-Pro-Hyp)4-Gly-Gly-amide, where the X- and Y-positions of the guest peptide are varied, have been used to examine the effect of changing Asn to Asp and Gln to Glu on triple-helix stability. This paper reports the stability of host-guest peptides containing the guest triplets Gly-Ala-Asn, Gly-Asn-Ala, Gly-Asn-Lys, Gly-Gln-Ala, Gly-Glu-Glu, and Gly-Leu-Glu.

Electrostatic interactions involving lysine make major contributions to collagen triple-helix stability.

Important stabilizing features for the collagen triple helix include the presence of Gly as every third residue, a high content of imino acids, and interchain hydrogen bonds. Host-guest peptides have been used previously to characterize triple-helix propensities of individual residues and Gly-X-Y triplets. Here, comparison of the thermal stabilities of host-guest peptides of the form (Gly-Pro-Hyp)3-Gly-X-Y-Gly-X'-Y'-(Gly-Pro-Hyp)3 extends the study to adjacent tripeptide sequences, to encompass the major classes of potential direct intramolecular interactions.

Stepwise construction of triple-helical heparin binding sites using peptide models.

The specific localization of the asymmetric form of acetylcholinesterase (AChE) in neuromuscular junctions results from the interaction of its collagen-like tail with heparan sulfate proteoglycans in the synaptic basal lamina. This interaction involves two heparin binding consensus sequences of the form XBBXB, where B is a basic residue, located in the triple-helical collagen tail: GRKGR for the N-terminal site and GKRGK for the C-terminal site. To explore the basis of the higher heparin affinity seen for the C-terminal site vs.

Triple-helix propensity of hydroxyproline and fluoroproline: comparison of host-guest and repeating tripeptide collagen models.

Peptide models have proved important in defining the structural features of the collagen triple-helix. Some models are based on multiple repeats of a given tripeptide unit, while a host-guest design includes an individual tripeptide unit substituted within a constant repeating Pro-Hyp-Gly framework. In the present study, proline, hydroxyproline, and fluoroproline residues are incorporated in X- or Y-positions of a guest triplet in the host-guest peptide design.

Structure and activity of D-Pro14 melittin.

D-Pro14 melittin was synthesized to investigate the effect of increasing the angle of the bend in the hinge region between the helical segments of the molecule. Structural analysis by nuclear magnetic resonance indicated that, in methanol, the molecule consisted of two helices separated at Pro14, as in melittin. However, the two helices in D-Pro14 melittin were laterally displaced relative to each other by approximately 7 A, and in addition, there was a small rotation of the carboxyl-terminal helix relative to the amino-terminal helix around the long axis of the molecule.

New insights into heparin binding to vitronectin: studies with monoclonal antibodies.

Vitronectin is a plasma glycoprotein that binds to a variety of ligands. There is considerable debate regarding the dependency of these binding interactions upon the conformational status of vitronectin, the role of multimerization and how the binding of different ligands can change vitronectin's conformational state. We have developed a method of capturing vitronectin directly from fresh plasma using solid-phase monoclonal antibodies.

Peptide investigations of pairwise interactions in the collagen triple-helix.

Pairwise interactions have been studied for the major secondary structures in proteins. The present work extends the characterization of interactions between side-chains to the context of a collagen triple-helix. In this study, the most frequent Gly-X-Y tripeptide sequences in collagen are characterized in terms of interchain interactions between non-imino acid X and Y residues, through the use of host-guest peptides and statistical frequency analysis.