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H J Carr

Publications and source records attributed to H J Carr.

5 recordsLinked to original sources

Scanning tunneling microscopy of a wheat seed storage protein reveals details of an unusual supersecondary structure.

Scanning tunneling microscopy has been used to demonstrate that a spiral structure based on beta-reverse turns is adopted by the repeat sequences present in a group of wheat gluten proteins. This structure is similar to the beta-spiral formed by a synthetic polypentapeptide based on a repeat sequence present in elastin. Wheat gluten and elastin are both elastomeric and it is possible that the spiral structure contributes to this property.

Journal Article↗

An investigation of the dissociation and denaturation of legumin by salts using laser light scattering and circular dichroism spectroscopy.

The dissociation of legumin, a 12 S seed storage globulin from Pisum sativum, has been studied by laser light scattering and circular dichroism spectroscopy. Salts from the Hofmeister series, in particular sodium perchlorate, were used as dissociating agents. The Mr 360,000 hexameric protein was found to dissociate first to trimers and further to monomers and the number of amino acids involved in the trimer-trimer interaction estimated to be 23(+/-4). Native legumin appears to be more strongly bound together than some analogous seed storage globulins from other plant species such as Arachis hypogaea or Sesamum indicum and the dissociation process was accompanied by some changes in conformation.

Circular Dichroism↗

Structure of tropomyosin-troponin T cocrystals.

Crystals formed from a mixture of tropomyosin and troponin T have an open double-stranded lattice structure with a diamond-shaped repeat. In some regions the appearance in electron micrographs of negatively stained specimens changes from this double-diamond lattice to a more condensed banded crystal form. The double-diamond lattice has plane group symmetry cmm with unit cell 76.3 by 21.7 nm. The molecules form continuous chains along the diagonal of the unit cell and the diagonal length (79.4 nm) is that expected for two tropomyosin molecules joined end-to-end. Computer filtering of the micrographs shows that the strands of the lattice are thicker from the acute vertex of the large diamond to a point about half-way along the side of the diamond, where there is a small blob of density. At the acute vertex of the diamond is a large blob of density which is accentuated, however, by being at the lattice node where strands cross each other, and which is much weaker in regions of the micrographs where the crystals have condensed laterally. The results indicate that troponin T is a long thin molecule running in contact with the tropomyosin strands over 40-50% of the tropomyosin molecular length. The small globular region may represent the end-to-end overlap of tropomyosin but is more likely to be a globular region at the C-terminal region of troponin T.

Animals↗