Showing papers in "International Journal of Biological Macromolecules in 1998"

TL;DR: This review will focus first on the present understanding of the structures of amylose and amylopectin and their organization within the granule, and then on the biosynthetic mechanisms explaining the biogenesis of starch in plants.

TL;DR: In this paper, 40 representative alpha-crystallin-small heat-shock protein (alpha-Hsp) superfamily is compared and their characteristic C-terminal 'alpha-crystalin domain' of 80-100 residues contains short consensus sequences that are highly conserved from prokaryotes to eukaryotes.

TL;DR: The results showed: the intrinsic viscosities decreased linearly with increasing temperature, therefore, a temperature-induced conformational transition did not occur for all 10 different molecular weight chitosans in the temperature range studied.

TL;DR: The effects of pH, ionic strength and heat on the structure of beta-lactoglobulin (beta-lg) have been investigated by studying the intrinsic tryptophan fluorescence of the protein, and what is believed to be the first front-face fluorescence measurements on globular protein gels are reported, showingeffects of pH and NaCl concentration.

TL;DR: This study reveals for the first time that there is a close relationship between the conformation of proteins and the mechanical properties of films.

TL;DR: Extractive-free cork from Quercus suber L was submitted to a solvolysis treatment with methanolic NaOH which yielded 37% (od cork) of suberin This mixture of compounds was thoroughly characterized by FTIR, 1 H- and 13 C-NMR, gas chromatography coupled with mass spectrometric analysis, vapour pressure osmometry (VPO), mass spectrography (MS) and gel permeation chromatography (GPC) as discussed by the authors.

TL;DR: It is proposed that alpha-crystallin adopts a two-domain structure with the larger C-terminal domain unfolding first in the presence of denaturant, and this model is combined into a model for the quaternary structure of alpha- Crystallin.

TL;DR: The effects of heat-treatment on the conformational changes of beta-lactoglobulin were monitored by differential scanning calorimetry (DSC), binding properties to 1-anilino-8-naphthalenesulphonic acid (ANS) and to 5,5'-dithio-bis (2-nitrobenzoic acid) (DTNB) were monitored and the role of hydrophobic interactions in the aggregation process of denatured beta-

TL;DR: The degradation of hyaluronan was followed by viscosimetry and by HPLC in order to study the possible role of Maillard products (lysine-glucose) on the alteration of the vitreous gel in aging and diabetes as discussed by the authors.

TL;DR: The restrictive role of polymer crystallinity on uranyl sorption capacity was confirmed and the formation of a unique type of complex was formed by the coordination with chitosan amino groups.

TL;DR: Manipulation of the electrostatic coat of the chitin could be a method of cellular remote control for formation of the helicoid in arthropod cuticle to allow the arthropods to set up conditions that aid the self assembly process.

TL;DR: The results suggested a more effective interaction of the galactomannan with disordered xanthan segments, which are more abundant in low salt concentrations but are still present in lower proportion at temperatures lower than the temperature of xantha conformational transition (Tm).

TL;DR: The overall secondary structure, the degree of oligomerization and the chaperone activity of Hsp25 seem independent of the formation of the intermolecular disulfide bond and only the stability of the hydrophobic N-terminal part of the molecule is influenced by formation of this bound.

TL;DR: In this paper, the effects of site-directed mutagenesis, the properties of naturally occurring aberrant forms of α-crystallin and the influence of chemical modifications were explored.

TL;DR: In this paper, the chaperone-like activity of α-crystallin towards photo-induced aggregation of β-and γ -crystallins was investigated and shown to be temperature-dependent.

TL;DR: The conformational preferences of the naturally occurring poly(γ-d -glutamic acid in the unionized state were investigated using a combination of molecular dynamics and quantum mechanical calculations as discussed by the authors.

TL;DR: Investigation of complex formation indicates that although stable complex formation between enzymes and α -crystallin may be involved in protection of enzymes against thermal inactivation, protection against chemically-induced inactivation may be more dynamic in nature.

TL;DR: Differences and complexities in α -crystallin phosphorylations are consistent with the idea that each polypeptide has distinctive structural and metabolic roles.

TL;DR: The outcome of solution scattering analyses of multidomain or oligomeric proteins is critically appraised, in particular the biological significance of structures determined by these solution scattering curve fits.

TL;DR: The results obtained showed that Trp-19 has an accessibility to the quenchers higher than could be supposed from its structural location, a fact that could be associated with a slight conformational change of the protein.

TL;DR: New details on the structure of beta-casein adsorbed layers, at the air-water interface, have been obtained using X-ray and neutron reflectivity and this distribution seems to be consistent with statistical theories established for flexible polymers.

TL;DR: The data suggest that the F27R mutation effected the thermal stability of alpha B-crystallin making it unstable at temperatures > or = 60 degrees C, and in agreement with the published work, at these temperatures the F 27R human recombinantalpha B- Crystallin does not protect the target protein from aggregation.

TL;DR: The physico-chemical properties and the quaternary structure features of alpha-crystallins that were demonstrated to control light scattering and transparency are recalled and a formal approach is proposed to design models for the alpha- Crystallin quaternARY structure, including the question of whether alpha-Crystallins assemble with symmetry.

TL;DR: The rheological properties of an unpasteurised and concentrated xanthan fermentation broth and the inhibition of the dissociation in two single strands in the high concentration range are attributed to the presence of nematic phases observed by viscoelastic measurements and apolar microdomains evidenced by the addition of a neutral detergent.

TL;DR: Aggregation properties of Gelatin chains in neutral aqueous solutions, are reported in the temperature range T = 35-60 degrees C, from the measured intrinsic viscosity, diffusion coefficient, D(o), molecular weight Mw, and radius of gyration (Rg) data.

TL;DR: Binding modalities of chlorpromazine and trifluoperazine, two widely used antipsychotic phenothiazine drugs with hemoglobin and myoglobin have been studied to understand how the quaternary, tertiary and secondary structural organisations of the proteins regulate the binding process.

TL;DR: The addition of linseed oil to the gamma-irradiated film matrix enhanced polymer recovery while minimizing chain scission and the formation of a higher crosslink density within the polymer matrix decreased the biodegradability of the PHA films.

TL;DR: Current knowledge concerning the effects of known posttranslational modifications upon the molecular chaperone properties and aggregation behavior of α -A and α -B crystallin are reviewed.

TL;DR: The results suggest that heat stability is a function of the protein's secondary structure and folding state, while chaperone-like activity is primarily afunction of factors at the tertiary and quaternary levels of organization.