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Terahertz time-domain spectroscopy of poly-L-lysine. 2010

Ohki Kambara, and Atsuo Tamura, and Takashi Uchino, and Kohji Yamamoto, and Keisuke Tominaga
Graduate School of Science and Technology, Kobe University, Nada, Kobe, Hyogo 657-8501, Japan.

Poly-L-lysine is known to have three different secondary structures depending on solvent conditions because of its flexible nature. In previous work (Kambara et al., Phys Chem Chem Phys 2008, 10, 5042-5044), we observed two different types of structural changes in poly-L-lysine. In the present study, we investigated the low-frequency spectrum of poly-L-lysine with a beta-sheet structure in the solid state by terahertz time-domain spectroscopy. On the basis of this spectroscopic analysis, we found that the low-frequency dynamics differed from those of other polypeptides. Furthermore, we performed powder X-ray diffraction measurement on poly-L-lysine, which was found to be highly amorphous compared with other polypeptides.

UI MeSH Term Description Entries
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D011107 Polylysine A peptide which is a homopolymer of lysine. Epsilon-Polylysine,Poly-(Alpha-L-Lysine),Epsilon Polylysine
D013816 Thermodynamics A rigorously mathematical analysis of energy relationships (heat, work, temperature, and equilibrium). It describes systems whose states are determined by thermal parameters, such as temperature, in addition to mechanical and electromagnetic parameters. (From Hawley's Condensed Chemical Dictionary, 12th ed) Thermodynamic
D017433 Protein Structure, Secondary The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to ALPHA-HELICES; BETA-STRANDS (which align to form BETA-SHEETS), or other types of coils. This is the first folding level of protein conformation. Secondary Protein Structure,Protein Structures, Secondary,Secondary Protein Structures,Structure, Secondary Protein,Structures, Secondary Protein
D055068 Terahertz Spectroscopy Spectrum analysis of absorbed or emitted TERAHERTZ RADIATION. Spectroscopy, Terahertz
D033362 Powder Diffraction Method of using a polycrystalline powder and Rietveld refinement (LEAST SQUARES ANALYSIS) of X-RAY DIFFRACTION or NEUTRON DIFFRACTION. It circumvents the difficulties of producing single large crystals. Diffraction, Powder

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