DC pole | Wartość | Język |
dc.contributor.author | Maciejowska, Anna | - |
dc.contributor.author | Godziek, Agnieszka | - |
dc.contributor.author | Sajewicz, Mieczysław | - |
dc.contributor.author | Kowalska, Teresa | - |
dc.date.accessioned | 2018-05-25T12:41:44Z | - |
dc.date.available | 2018-05-25T12:41:44Z | - |
dc.date.issued | 2017 | - |
dc.identifier.citation | Reaction Kinetics, Mechanisms and Catalysis, Vol. 120, iss. 2 (2017), s. 421-437 | pl_PL |
dc.identifier.issn | 1878-5190 | - |
dc.identifier.uri | http://hdl.handle.net/20.500.12128/4009 | - |
dc.description.abstract | The non-linear dynamics of spontaneous peptidization running in 10 monocomponent and binary abiotic liquid systems of L- and D-Ala and L- and D-Phe is investigated with use of turbidimetry with continuous registration, high-performance liquid chromatography with light scattering detection (HPLC-ELSD), mass spectrometry (MS), and spectroscopy of far UV circular dichroism (CD). The turbidity patterns represent a sum of the light scattering effects caused by insoluble peptides of unknown yields, structures, and molecular weights. The auxiliary analytical techniques confirm the non-linear nature of peptidization (HPLC-ELSD) and spontaneous formation of the homo- and heteropeptides (MS). CD spectroscopy seems to confirm the presence of the secondary α-helix structures. The similarity of turbidity patterns is revealed with the monocomponent (L or D) and binary (L-L or D-D) systems of equichiral α-amino acids, and dissimilarity of patterns is observed with the binary systems of inequichiral α-amino acids (L-D). The tentative conclusion is drawn that the peptides assembled of equichiral α-amino acid units are able to assume the secondary (right- or left-handed α-helix) structures, which in a certain way could foster the similarity of turbidity patterns, and the peptides built of inequichiral α-amino acid units cannot ensure an efficient enough stringing of monomer molecules into equichiral heptades to form complete segments of an α-helix. This randomness of the α-amino acids arrangement in the inequichiral peptide molecules most probably manifests itself as a lack of similarity among the respective turbidity patterns | pl_PL |
dc.language.iso | en | pl_PL |
dc.rights | Uznanie autorstwa 3.0 Polska | * |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/pl/ | * |
dc.subject | Alanine | pl_PL |
dc.subject | Phenylalanine | pl_PL |
dc.subject | Secondary peptides structure | pl_PL |
dc.subject | Spontaneous peptidization | pl_PL |
dc.subject | Turbidimetric measurements | pl_PL |
dc.subject | α-Helices | pl_PL |
dc.title | Turbidity patterns of spontaneous peptidization in an aqueous abiotic system and possible secondary peptide structures | pl_PL |
dc.type | info:eu-repo/semantics/article | pl_PL |
dc.identifier.doi | 10.1007/s11144-017-1157-3 | - |
Pojawia się w kolekcji: | Artykuły (WNŚiT)
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