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T B Khromova

Publications and source records attributed to T B Khromova.

5 recordsLinked to original sources
PubMed1992

Bound water in the collagen-like triple-helical structure.

The ir amide bands of the triple-helical polytripeptides and collagens upon hydration of films are investigated. On the basis of our assignment of the amide I components, the formation of hydrogen bonds between the peptide backbone and structural water is studied. The C1O1--HOH hydrogen bonds are found more ordered than the C3O3--HOH hydrogen bonds. The specific incorporation of water in the triple helix is followed by multistep conformational changes and by increasing of the interpeptide hydrogen-bond strength. The formation of the polypeptide hydrate structure depending on the amino acid composition and the chain length is examined.

Amino Acid Sequence↗
PubMedDate not supplied

[Formation of a hydrate structure in the collagen-like triple helix upon hydration].

By the IR-spectroscopy method successive stages of hydrate envelope formation of the collagen-like triple-helical structure of the monodisperse synthetic polytripeptide Z-(Gly-Pro-Pro)8-OMe were studied. The multistep-type process is followed by isomorphic transitions of the triple-helical structure and by the increasing of hydrogen bond strength.

Collagen↗
PubMedDate not supplied

[Aggregation of poly-L-proline in aqueous solution].

Infrared spectra were measured for both aqueous (D2O) solution and the solid state of form II poly-L-proline in the amide I region as a function of the temperature. The temperature range includes the region where a precipitation is known to occur. From the analysis of spectra of hydrated films and aqueous solutions at different temperatures one can see that there are some peptide C = O-groups which are bounded with water. From this study it has been concluded that poly-L-proline exists in aggregate form even at temperatures lower that required for precipitation. It is supposed that poly-L-proline forms the aggregates including at least 40--50 polypeptide chains with hexagonal packing. At heating crystallisation of such aggregates occurred and it causes precipitation of poly-L-proline II.

Kinetics↗
PubMedDate not supplied

[Thermodynamic studies of triple-helical structures of the collagen type in oligotripeptides during study of molecular chain elongation].

The conformational transition collagen-like triple helix in equilibrium with chains of oligotripeptides Z-(Gly-Pro-Pro)n-OMe with n = 6, 7, 8 in water by variation of solution temperature and sample concentration has been studied using IR-, CD-spectroscopy and microcalorimetry methods. The straight line correlation between the obtained value of the transition enthalpy and entropy and the number of the triplets (3n - 2), involved in the interpeptide set of hydrogen bonds was revealed. Evidently the effect of terminal groups is really weak in this case, and the interpeptide bonds of the triple helix may be regarded as equivalent one another. The estimated cooperative block of nucleation corresponds in length to the one full turn of the superhelix. The state diagrams of the oligotripeptides with n = 6, 7, 8 in aqueous solution are presented.

Collagen↗