Sex- and/or ethnic-appropriate echocardiographic reference values are indicated for many measurements of LA and LV size, LV mass, and EF. Reference values for LV volumes and mass also differ across the age range.

Proteins from the GASA/snakin superfamily are common in plant proteomes and have diverse functions, including hormonal crosstalk, development, and defense. One 63-residue member of this family, snakin-1, an antimicrobial protein from potatoes, has previously been chemically synthesized in a fully active form. Herein the 1.5 Å structure of snakin-1, determined by a novel combination of racemic protein crystallization and radiation-damage-induced phasing (RIP), is reported. Racemic crystals of snakin-1 and quasi-racemic crystals incorporating an unnatural 4-iodophenylalanine residue were prepared from chemically synthesized d- and l-proteins. Breakage of the C-I bonds in the quasi-racemic crystals facilitated structure determination by RIP. The crystal structure reveals a unique protein fold with six disulfide crosslinks, presenting a distinct electrostatic surface that may target the protein to microbial cell surfaces.

Supporting information and the ORCID identification number(s) for the author(s) of this article can be found under http://dx.These are not the final page numbers! Ü Ü Scheme 1. Synthetic strategy for the preparation of l-snakin-1 (5), iodo-l-snakin-1 (6), and d-snakin-1 (7).

propyl]cysteine (Pam 2 Cys) is a synthetic lipid motif known to act as a TLR2 agonist when incorporated into peptide vaccines. Herein, we report the synthesis of Pam 2 Cys-containing, propargyl-functionalised 'clickable' building blocks and their conjugation with azide-functionalised antigenic peptides using click chemistry. This method facilitates the fully convergent preparation of self-adjuvanting lipopeptides for use as vaccines.

Members of the Chordopoxvirinae subfamily possess an unusual 11 protein entry-fusion complex (EFC) that is highly conserved and present in all species. The mode of action of this EFC is unknown, and the interactions of the constituent proteins are uncharacterised. Here, we present the chemical synthesis of membrane domain truncated linear constructs of two EFC proteins in orf virus, ORFV036 and 049. By using Boc solid phase peptide synthesis and native chemical ligation methods, these truncated proteins have been readily prepared in milligram quantities. These robust synthetic protocols allow ready access to these polypeptides to facilitate biological studies.