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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Il nuovo cimento della Società Italiana di Fisica 5 (1985), S. 516-526 
    ISSN: 0392-6737
    Keywords: Molecular biophysics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Description / Table of Contents: Riassunto Il marchio di spin TEMPO non mostra un legame con la molecola di mioglobina in soluzione. Ciò è probabilmente dovuto al fatto che questa proteina non ha una tasca idrofobica abbastanza grande per sistemare la molecola TEMPO. Nel cristallo il marchio di spin è legato e si osservano due tipi di spettro: uno isotropo e l'altro anisotropo. Il tempo di correlazione per il marchio nel cristallo è molto sensibile alla temperature mostrando una transizione vicino a 30 °C. Questo cambiamento può essere spiegato come un risultato del cambio di conformazione osservato per la mioglobina vicino a questa temperatura: il movimento del marchio di spin diventa piú ristretto al di sotto di questa temperature. Un cambiamento di idratazione è la probabile causa di questo cambiamento strutturale. I cambiamenti negli spettri EPR del marchio anisotropo suggeriscono che esso sia legato vicino ai primi strati di proteina nel cristallo.
    Notes: Summary The spin label TEMPO does not show a binding to myoglobin molecule in solution. This is probably due to the fact that this protein does not have a hydrophobic pocket large enough to accommodate the TEMPO molecule. In the crystal the spin label is bound and two kinds of spectra are observed: one isotropic and the other anisotropic. The anisotropic site is probably an intermolecular one. The correlation time for the label in the crystal is very sensitive to temperature showing a transition near 30 °C. This change can be explained as a result of the conformational change observed for myoglobin near this temperature: the motion of the spin label becomes more restricted below this temperature. Change in hydration is the probable cause of this structural change. The changes in the EPR spectra of the anisotropic label suggest that it is bound near the first layers of protein in the crystal.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Il nuovo cimento della Società Italiana di Fisica 7 (1986), S. 139-150 
    ISSN: 0392-6737
    Keywords: Molecular biophysics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Description / Table of Contents: Riassunto La mioglobina di tartaruga marina è state marcata con spin label maleimida nella forma cianometa (MbT-CN) e cambiamenti di temperatura sono stati indotti e accompagnati per EPR. Lo spettro di EPR è composto da un segnale fisso e un’altro piú mobile. Comparazioni di questo spettro con altri ottenuti da altre proteine, bloccando l’NH2 terminale e titolando il gruppo SH, mettono in evidenza che un’istidina reattiva partecipa alla marcazione dello spin label. I nostri risultati nei cambiamenti di temperatura indotti e accompagnati dallo spin label indicano che la sequenza di fatti ha indotto una transizione che porta alla denaturazione della proteina (predenaturazione): con aumento della temperature apH=8.5, il parametro di EPR per il segnale fisso (α EPR) è il primo a rivelare il cambiamento strutturale (T 1/2=28°C), allora il segnale mobile si modifica (T 1/2=44°C) e infine il centro attivo accompagnato per l’assorbimento ottico del ferro subisce questo cambiamento (T 1/2=64°C). L’energia di attivazione calcolata per lo spettro mobile è intorno di 3 kcal/mol indicando che questo cambiamento è piccolo quando comparato con la variazione di entalpia ottenuta per l’assorbimento ottico del ferro (40 kcal/mol). Questa predenaturazione che avviene nella fascia da 30 a 50°C sembra essere una proprietà comune delle mioglobine, come è stato osservato anche per la mioglobina di balena e di aplisia.
    Abstract: Резюме В миоглобин морской черепахи вводится спиновая метка в форму (MbT-CN) и методом EPR контролируются термоиндуцированиые изменения. Спектр EPR составляют неподвижные и более подвижные сигналы. Сравнение этого спектра со спектрами других белков, блокирование концевой NH2-группы и титрование SH-групп приводит к выводу, что помечены активные гистидины. Наши результаты по наблюдению за термоиндуцированными изменениями дают возмож-ность предположить, что имеет место последовательность событий в процессе перехода, который приводит к денатурации белка (пред-денатурация): с увеличением температуры приpH=8.5 параметр EPR для неподвижного сигнала (α EPR) первым регистрирует структурное изменение (T 1/2=28°C); затем изменяется подвижный сигнал (T 1/2=44°C) и, наконец, претерпевает изменения активный центр, который мониторируется за счет оптического поглощения в железе (T 1/2=64°C). Энергия активации, вычисленная на основе подвижного спектра, составляет примерно 3 ккал/моль. Это указывает на то, что указанные изменения являются весьма тонкими по свавнению с изменениями энтальпии, которая мониторируется за счет оптического поглощения в железе (40 ккал/моль). Эти явление пред-денатурации, которое наблюдается в области (30÷50)°C, по видимому, представляет общее свойство миоглобинов.
    Notes: Summary A sea turtle myoglobin has been spin labelled in the cyanomet form (MbT-CN) with a maleimide spin label and temperature-induced changes were monitored by EPR. The EPR spectrum is composed by an immobilized and a more mobile signal. Comparison of this spectrum with spectra obtained from other proteins, blocking of the NH2-terminal and titration of SH groups lead to the conclusion that a reactive histidine is involved in the spin labelling. Our results on the temperature-induced changes monitored by the maleimide spin label suggest that a sequence of events is taking place in the transition which leads to protein denaturation (predenaturation): with increase in temperature atpH 8.5 the EPR parameter for the immobilized signal (α EPR) is the first to report the structural change (T 1/2=28°C); then the mobile signal changes (T 1/2=44°C) and finally the active centre monitored by optical absorption of the iron heme undergoes these changes (T 1/2=64°C). The activation energy calculated from the mobile spectrum is around 3 kcal/mol showing that these changes are quite subtle if compared to the enthalpy changes monitored by optical absorption of iron (40 kcal/mol). This predenaturation occurring in the range (30÷50)°C seems to be a general property of myoglobins, as has been observed also for whale and applysia.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Il nuovo cimento della Società Italiana di Fisica 9 (1987), S. 227-245 
    ISSN: 0392-6737
    Keywords: Electron paramagnetic resonance and relaxation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Description / Table of Contents: Riassunto Si riportano gli spettri ESR per un radicale nitrossido stabile 4-idrossi-2, 2, 6, 6-tetrametil-piperidina-1-ossile (TANOL) introdotto come impurità in una matrice di struttura nota, 4-idrossi-2, 2, 6, 6-tetrametilpiperinadi (1) nelle bandeX eQ. L'uso del nitrossido predeuterato ha mostrato un considerabile miglioramento nella risoluzione degli spettri ESR per moltissime orientazioni nel cristallo. Si studiano le interazioni dei protoni nei pressi del gruppo paramagnetico N−O e si determinano i tensori superiperfini per due protoni con accoppiamento forte: uno di questi protoni è legato con l'idrogeno al N−O ad una distanza di 2.09 Å. I valori principali del tensore sono −5.2; +5.4; e −5.1 G. Il secondo protone è molto spostato dall'elettrone ed è certamente non coinvolto in un legame a idrogeno. I valori principali sono in questo caso 2.0, −1.7, −2.7 G. L'assea del cristallo à una direzione principale per tutti i tensori magnetici per il TANOL in questo sistema.
    Abstract: Резюме Приводятся ESR спектры для устойчивого радикала окиси сзота TANOL, введенного, как примесь, в матрицу известной структуры вX- иQ-зону. Использование передейтерированной окиси азота обнаруживает значительное улучшение разрешения в ESR спектрах для большинства ориентаций в кристалле. Исследуется взаимодействие протонов в окрестности параметрической группы N−O. Определяются сверхтонкие тензоры для двух сильно связанных протонов: один из этих протонов представляет водород, связанный с N−O на расстоянии 2.09 Å. Главные значения этого тензора представляют −5.2, +5.4, −5.1 гаусс. Второй протон находится довольно далеко от электрона и не включается в водородную связь. В этом случае главные значения тензора равны 2.0, −1.7, −2.7 гаусс. Кристаллическая осьa представляет главное направление для всех магнитных тензоров для TANOL в этой системе.
    Notes: Summary ESR spectra are reported for a stable nitroxide radical 4-hydroxy-2, 2, 6, 6-tetramethyl-piperidine-1-oxyl (TANOL) introduced as impurity in a matrix of known structure, 4-hydroxy-2, 2, 6, 6-tetramethylpiperidine atX- andQ-band. The use of the perdeuterated nitroxide showed a considerable improvement in ESR spectra resolution for most orientations in the crystal. The interactions of protons in the neighbourhood of the paramagnetic group N−O were studied and the superhyperfine tensors for the two strongly coupled protons were determined: one of these protons is hydrogen-bonded to the N−O at a distance of 2.09 Å. The principal values of the tensor are −5.2; +5.4; −5.1 G. The second proton is further away from the electron and is certainly not involved in hydrogen bond. The principal values are in this case 2.0, −1.7, −2.7 G. Thea crystal axis is a principal direction for all magnetic tensors for TANOL in this system.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 1189 (1994), S. 243-246 
    ISSN: 0005-2736
    Keywords: Anesthetic ; Dibucaine ; Fluorescence stearic acid with a doxyl group at the nth carbon atom of the ; Local anesthetic ; Sarcoplasmic reticulum vesicle
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 1189 (1994), S. 74-80 
    ISSN: 0005-2736
    Keywords: Interaction ; Micelle ; NMR ; Papaverine ; Surfactant ; Vasodilator drug
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 1190 (1994), S. 319-328 
    ISSN: 0005-2736
    Keywords: Dibucaine ; Fluorescence spectroscopy ; Local anesthetic ; Micelle
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 944 (1988), S. 185-190 
    ISSN: 0005-2736
    Keywords: Chlorpromazine ; ESR ; Micelle ; Phase transition ; Spin label
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 0550-3213
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy Section 50 (1994), S. 1047-1056 
    ISSN: 0584-8539
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 0020-1693
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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