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dc.contributor.authorKostrikis, Leontios G.en
dc.contributor.authorLiu, D. J.en
dc.contributor.authorDay, L. A.en
dc.creatorKostrikis, Leontios G.en
dc.creatorLiu, D. J.en
dc.creatorDay, L. A.en
dc.date.accessioned2019-11-04T12:52:13Z
dc.date.available2019-11-04T12:52:13Z
dc.date.issued1994
dc.identifier.urihttp://gnosis.library.ucy.ac.cy/handle/7/53199
dc.description.abstractData have been obtained for the Pfl virion that establish its stoichiometry and conformational features of its DNA and its protein. The absorbance spectrum of the dissociated virus under alkaline denaturing conditions is fit exactly by spectra for DNA and protein at a mole ratio of one nucleotide per protein subunit. This result, together with three previous values by independent methods, establishes that the nucleotide/subunit ratio (n/s) of Pfl is unity. The absorbance spectrum of DNA in the intact native virus is assigned as the spectrum for heat denatured Pfl DNA, with ϵ(P) = 8400 M−1 cm−1 at 259 nm. The absorbance spectrum assigned to protein (two tyrosines) in the intact virus has 〈ϵ(Y)〉 = 2500 M−1 cm−1 per tyrosine at λmax of 281.5 nmen
dc.description.abstractthis is the most red-shifted and hyperchromic tyrosine spectrum known. The CD spectrum of the intact virus from 250 to 320 nm has no apparent DNA contribution, but has a strong contribution from the red-shifted tyrosine(s). The CD spectrum from 185 to 250 nm has the shape of α-helical CD reference spectra, but is perceptibly blue-shifted, with a crossover from negative to positive ellipticity at 199.7 nm, and it has very high amplitudes (e.g. [θ207.5nm] = -44 000 deg cm2 dmol−1). This spectrum indicates completely helical protein in the virus, with a predominance of α-helix and perhaps some 310-helix. The unit n/s ratio, the high absorbance and negligible near-UV CD for the DNA bases, and the high amplitudes for the helical protein are critical input data for the determination of Pf1 virus structure. © 1994, American Chemical Society. All rights reserved.en
dc.sourceBiochemistryen
dc.source.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-0028213921&doi=10.1021%2fbi00173a011&partnerID=40&md5=6de2e246fbe989c7e25b3d1b7cd6a56e
dc.subjectarticleen
dc.subjectpriority journalen
dc.subjectgeneen
dc.subjectamino acid sequenceen
dc.subjectnonhumanen
dc.subjectelectron microscopyen
dc.subjectViral Proteinsen
dc.subjectvirus proteinen
dc.subjectNucleic Acid Denaturationen
dc.subjectstoichiometryen
dc.subjectamino aciden
dc.subjectultraviolet radiationen
dc.subjectHydrogen-Ion Concentrationen
dc.subjectvirionen
dc.subjectSupport, Non-U.S. Gov'ten
dc.subjectDNA, Viralen
dc.subjectSupport, U.S. Gov't, P.H.S.en
dc.subjectDNA, Single-Strandeden
dc.subjecttyrosineen
dc.subjectdna sequenceen
dc.subjectHeaten
dc.subjectnucleotideen
dc.subjectInovirusen
dc.subjectvirus dnaen
dc.subjectcircular dichroismen
dc.subjectdna baseen
dc.subjectdna structureen
dc.subjectLighten
dc.subjectlight scatteringen
dc.subjectProtein Denaturationen
dc.subjectProtein Structure, Secondaryen
dc.subjectpseudomonas aeruginosaen
dc.subjectScattering, Radiationen
dc.subjectSpectrophotometry, Ultravioleten
dc.subjectvirusen
dc.subjectvirus morphologyen
dc.titleUltraviolet Absorbance and Circular Dichroism of Pf1 Virus: Nucleotide/Subunit Ratio of Unity, Hyperchromic Tyrosines and DNA Bases, and High Helicity in the Subunitsen
dc.typeinfo:eu-repo/semantics/article
dc.identifier.doi10.1021/bi00173a011
dc.description.volume33
dc.description.startingpage1694
dc.description.endingpage1703
dc.author.facultyΣχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences
dc.author.departmentΤμήμα Βιολογικών Επιστημών / Department of Biological Sciences
dc.type.uhtypeArticleen
dc.description.notes<p>Cited By :29</p>en
dc.source.abbreviationBiochemistryen
dc.contributor.orcidKostrikis, Leontios G. [0000-0002-5340-7109]
dc.gnosis.orcid0000-0002-5340-7109


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