T
Timo Lotta
Researcher at Orion Corporation
Publications - 11
Citations - 1288
Timo Lotta is an academic researcher from Orion Corporation. The author has contributed to research in topics: Fourier transform infrared spectroscopy & Infrared spectroscopy. The author has an hindex of 7, co-authored 11 publications receiving 1248 citations.
Papers
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Journal ArticleDOI
Kinetics of human soluble and membrane-bound catechol O-methyltransferase: a revised mechanism and description of the thermolabile variant of the enzyme.
Timo Lotta,Jukka Vidgren,Carola Tilgmann,I. Ulmanen,Krister Melén,Ilkka Julkunen,Jyrki Taskinen +6 more
TL;DR: Comparison of velocity parameters, substrate selectivity, and regioselectivity of the methylation of both enzyme forms, and a revised mechanism for the reaction cycle are discussed.
Journal ArticleDOI
PLS modelling of structure-activity relationships of catechol O-methyltransferase inhibitors.
TL;DR: The models reveal that inhibition activity is nonlinearly related to the size of the R5 substituent and its lipophilicity is important in the binding of inhibitors, while ionized R1 substituents decrease inhibition activity.
Journal ArticleDOI
Characterization of Langmuir-Blodgett films of 1,2-dipalmitoyl-sn-glycero-3-phosphatidylcholine and 1-palmitoyl-2-[10-(pyren-1-yl)decanoyl]-sn-glycero-3-phosphatidylcholine by FTIR-ATR
TL;DR: The pyrene-labelled phosphatidylcholine analogue, PPDPC, behaved differently from DPPC, and an ordering process was found in DPPC films when the number of the transferred layers was increased from one to five, as judged by the IR spectra.
Journal ArticleDOI
Fourier transform infrared study of fully hydrated dimyristoylphosphatidylglycerol. Effects of Na+ on the sn-1' and sn-3' headgroup stereoisomers.
TL;DR: It is demonstrated that Na+ binds tightly to 3'-DMPG, leading to the immobilization of the entire phospholipid polar headgroup, and thus reveals reduced motional freedom.
Patent
Compounds for deactivating phospholamban function on Ca-ATPase (phospholamban inhibitors)
Piero Pollesello,Martti Ovaska,Jukka Tenhunen,Jukka Vidgren,Marjo Yliperttula-Ikonen,Carola Tilgmann,Timo Lotta,Juha Kaivola +7 more
TL;DR: In this article, the three-dimensional structure of the cytosolic domain of the PLB and its active site were determined from NMR data of sufficiently high resolution for the 3D structure determination.