Niels H. Andersen

TL;DR: As the smallest protein-like construct, Trp-cage miniproteins should provide a testing ground for both experimental studies and computational simulations of protein folding and unfolding pathways.

TL;DR: Previously undescribed stable isotope determinations of charred cereals and pulses from 13 Neolithic sites across Europe show that early farmers used livestock manure and water management to enhance crop yields and suggest that commonly applied paleodietary interpretations of human and herbivore δ15N values have systematically underestimated the contribution of crop-derived protein to early farmer diets.

TL;DR: A detailed analysis of backbone amide NH chemical shift temperature gradients for proteins and highly cross-linked peptides reveals that hydrogen-bonded exchange-protected NHs are characterized by Δδ/ΔT values of −2.0 ± 1.4 ppb/°C while exposed NHs typically display gradients of −6.0 → −8.5 ppb /°C; however, numerous exceptions to these generalizations occur.

TL;DR: The structuring preferences of exendin-4 and GLP-1 are determined by NMR in both the solution and dodecylphosphocholine (DPC) micelle-associated states; both peptides display significant helicity from residue 7 to residue 28 with greater fraying at the N-terminus, and secondary structure definition from chemical shift deviations may be the most appropriate treatment for peptides that lack tertiary structure.

TL;DR: A mutational study of the peptide corresponding to the second hairpin of the protein G B1 domain (GB1p) provided a series of mutants with significantly increased fold stability, based on improvement of the direction-reversing loop and the addition of favorable Coulombic interactions at the sequence termini.