Determinations of gravity / by C.S. Wright.

Abstract

The auxiliary adjustable pendulum is used only to determine the flexure correction for No. 21 and, for this, its period of vibration is adjusted till it is approximately equal to that of No. 21.

1H NMR study of the interaction ofN,N′,N″‐triacetyl chitotriose with Ac‐AMP2, a sugar binding antimicrobial protein isolated fromAmaranthus caudatus

“…Indeed, all residues with significant shifts in Ac-AMP2 are located in a common Cys-Cys-Ser-Gln-Aro-Gly-Aro-Cys-Gly-(Xxx)nTyr-Cys sequence (with Aro coding for either Tyr, Trp of Phe). In hevein and WGA, these residues are found in close spatial proximity and constitute the binding site for N,N',N"-triacetyl chitotriose [4,6,15]. From our titration data and the observed intermolecular NOEs between the aromatic moieties of Phe ~8, Tyr 2° and Tyr 27 with the N,N'-N"-triacetyl chitotriose resonances we therefore conclude that Ac-AMP2 has a similar sugar binding site.…”

“…The sequence is very similar to that of the protein hevein (isolated from rubber tree latex) which folds into a 'toxin-agglutinin fold' or 'hevein domain' [2]. Structure determination of hevein by ~H NMR [3] and of WGA by X-ray diffraction [4] have shown that the WGA domains and hevein have a common structural fold. Although considerably shorter, Ac-AMP2 displays strong sequence homology with parts of hevein and the hevein-like domains ( Fig.…”

Structural features of plant chitinases and chitin‐binding proteins

“…Typical class I chitinases consist of an N-terminal chitin-binding hevein domain followed by a chitinase domain and a vacuolar targeting sequence [21] which is cleaved off during processing of the proprotein [22]. Three-dimensional structures have been determined for the hev- ein domain in hevein and WGA [7,8,11] and for barley chitinase CH126, which consists of only one single domain [9]. Disulfide bridges are very well conserved structural features in extracellular and other proteins synthesized at the rough endoplasmic reticulum [23], and conserved positions of Cys residues in chitinases can be taken as evidence of identically located disulfide bridges or free cysteine residues.…”

Crystallization and preliminary X‐ray data for peanut agglutinin

“…The chemical nature of the differences among these isolectins is not known; however, it must be slight since the diffraction pattern extends past 2.8 A resolution. Wheat germ agglutinin was also crystallized in a form that contained more than one isolectin, and these crystals were used to determine its structure [20].…”