Mapping the Three-Dimensional Structure of Proteins by Photochemical Techniques

Jori, Giulio; Spikes, John D.

doi:10.1007/978-1-4684-2580-2_6

Cited by 15 publications

(2 citation statements)

References 316 publications

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“…It damages the DNA and RNA of bacteria, viruses and other pathogens and thus destroys their ability to multiply and cause disease. It does this by eliciting single photon photochemical effects in nucleic acids through forming covalent bonds between certain adjacent bases [5]. This modification results in incorrect codes being transmitted from the nucleic acids and causes irreversible damage to the microorganisms.…”

Section: Discussionmentioning

confidence: 99%

Exposure of rabbits to ultraviolet light-inactivated rabbit haemorrhagic disease virus (RHDV) and subsequent challenge with virulent virus

2005

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This study investigated whether exposure to inactivated rabbit haemorrhagic disease virus (RHDV) can produce an antigenic response in rabbits and protect them from a subsequent challenge with virulent virus. The aim was to determine if the spreading of baits containing RHDV, which is a common management practice in New Zealand to reduce rabbit numbers, could result in protective immunity in wild rabbits. RHDV was inactivated by ultraviolet (UV) light using an electronic UV crosslinker with a UV dose of 168.48 W-s/cm2 and a UV intensity of 0.0078 W/cm2. Two groups of four rabbits were then inoculated with inactivated virus via oral and intramuscular routes. Rabbits were monitored for 30 days post-inoculation and then challenged orally with virulent virus. No rabbit exposed to inactivated RHDV developed clinical signs of RHD or had antibodies at day 30 post-infection and all animals died within 82 h after challenge with virulent virus. No antibodies were detected at the time of death. These findings suggest that exposure to virus completely inactivated by UV light in the field or on baits will not protect rabbits against challenge with virulent virus.

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Section: Discussionmentioning

confidence: 99%

Exposure of rabbits to ultraviolet light-inactivated rabbit haemorrhagic disease virus (RHDV) and subsequent challenge with virulent virus

2005

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“…The nucleosomes are connected through a z 60-base-pair stretch of DNA associated with the last histone, H1 [1,2]. However, in the living cell only a small fraction of the chromatin is in an active state, and recent reports based on enzyme-digestion studies indicate that this part may be physically different from bulk chromatin In order to study the changes in chromatin structure and conformation on a molecular level, we have started a program utilizing photoaffinity probes [9,10] as tools, aiming to construct photoactive molecules which bind tightly, and preferably in a sequence-specific manner, to DNA. As a first step towards this goal we now describe the syntheses and some biochemical properties of a number of azidoaryl derivatives of 9-aminoacridine, and show that these compounds fulfil some of the requirements desired of such photolabels.…”

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confidence: 99%

Photoaffinity Labeling of Chromatin

Nielsen¹

1982

European Journal of Biochemistry

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The syntheses and properties of potential photoaffinity labels for the proteins in chromatin studies are described. One compound, N , N'-bis-(9-acridinyl)-4-aza-4-(4-azidobenzoyl)-1,7-diaminoheptane dihydrochloride, has been studied more closely. This photolabel shows high affinity towards DNA (K, z 3 x lo5 M-') and photoreacts with histones at wavelengths in the range 260-450 nm. The photoreaction was monitored fluorimetrically, and labeling of histones HI, H2A/H2B and H3 was observed. When chromatin was photolabeled, labeling of HI was exclusively quenched by NaCl at concentrations which are known to cause dissociation of this histone from the DNA. It is thus inferred that only DNA-associated proteins are photolabeled by the reagent.It has been shown that the major part of the chromatin in eucariotic cells is organized in subunit repeats (nucleosomes) of 145 base pairs wrapped around a core of two of each of the histones H2A, H2B, H3 and H4. The nucleosomes are connected through a z 60-base-pair stretch of DNA associated with the last histone, H1 [1,2]. However, in the living cell only a small fraction of the chromatin is in an active state, and recent reports based on enzyme-digestion studies indicate that this part may be physically different from bulk chromatin In order to study the changes in chromatin structure and conformation on a molecular level, we have started a program utilizing photoaffinity probes [9,10] as tools, aiming to construct photoactive molecules which bind tightly, and preferably in a sequence-specific manner, to DNA. As a first step towards this goal we now describe the syntheses and some biochemical properties of a number of azidoaryl derivatives of 9-aminoacridine, and show that these compounds fulfil some of the requirements desired of such photolabels.[3 -81. MATERIALS AND METHODSUltraviolet spectra were recorded on a Pye Unicam SP 1800 spectrophotometer and infrared spectra on a PerkinElmer PE 580 spectrophotometer. Fluorescence spectra were obtained on a Perkin-Elmer MPF 3 or an Aminco-Bowman spectrofluorometer. Dyes used for fluorimetry or photoaffinity labeling experiments were freed from contaminating acridone by passing a methanol solution of the dye (100 pg in 100 pl methanol) through a column (5 x 50 mm) of Sephadex LH 20 (Pharmacia). The acridone is retarded more than the 9-aminoacridines when eluted with methanol. Calf thymus DNA was purchased from Sigma. ( I ) . A mixture of 450 mg of compound 7, 450 mg 9-chloroacridine and 1 g phenol was heated at IOO' C for 30 niin. After cooling, the product was precipitated with 50 ml diethyl ether: 850 mg (95 %). Recrystallization from methanol containing 1 % HCI yielded the pure compound.

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Das Diazo‐chinon von PQQ als mögliches Reagenz für die Kartierung von Chinoproteinen mittels Photoaffinitätsmarkierung

Martin¹,

Winkler²

1993

Helvetica Chimica Acta

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The Diazo-quinone of P Q Q as a Possible Reagent for Mapping Quinoproteins by Photo-affinity Labeling PQQ is an organic redox cofactor found in a class of enzymes called quinoproteins. The synthesis and the photochemistry of the diazo-quinones of PQQ and PQQ-triester are described. The photogenerated Wo(ff--rearrangement products have been caught with water and methanol as model nucleophiles. The products show a strong fluorescence. The diazoquinone of PQQ may be considered as a possible reagent for mapping quinoproteins by photo-affinity labeling. Im Falle von PQQ ist es naheliegend, die photoreaktive Gruppe nicht oiu Spacer an das Coenzym anzuhangen, sondern P Q Q direkt in sein eigenes Diazid der Formel 2 zu iiberfiihren. Bei der Belichtung sollte uber die Wolff-Umlagerung das ringverengte Keten 3 entstehen, welches durch eine nucleophile Gruppe (proteingebundenes OH, NH, SH) in

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Mapping the Three-Dimensional Structure of Proteins by Photochemical Techniques

Cited by 15 publications

References 316 publications

Exposure of rabbits to ultraviolet light-inactivated rabbit haemorrhagic disease virus (RHDV) and subsequent challenge with virulent virus

Exposure of rabbits to ultraviolet light-inactivated rabbit haemorrhagic disease virus (RHDV) and subsequent challenge with virulent virus

Photoaffinity Labeling of Chromatin

Das Diazo‐chinon von PQQ als mögliches Reagenz für die Kartierung von Chinoproteinen mittels Photoaffinitätsmarkierung

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