Raman spectra and structure of a 25mer HCV RNA

Carmona, Pedro; Molina, Marina; Rodrı́guez-Casado, Arantxa

doi:10.1002/jrs.2192

Cited by 11 publications

(10 citation statements)

References 36 publications

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“…It consists of 58 amino acids including three disulfide bridges. Moreover, this protein is highly stable and very resistant toward denaturation . The first comprehensive studies on TIP were carried out by Brunner et al with the use of 488 nm laser, but also the FTRS analysis of TIP thermal stability and conformation was published .…”

Section: Resultsmentioning

confidence: 99%

Raman spectroscopy of proteins: a review

Ryguła

Majzner

Marzec

et al. 2013

J Raman Spectroscopy

876

790

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In this work, 26 proteins of different structure, function and properties are investigated by Raman spectroscopy with 488, 532 and 1064 nm laser lines. The excitation lines were chosen in NIR and Vis range as the most common and to show the difference due to normal and resonance effect, sometimes accompanied by the fluorescence. The selected proteins were divided, according to the Structural Classification of Proteins, into four classes according to their secondary structure, i.e. α‐helical (α), β‐sheet (β), mixed structures (α/β, α + β, s) and others. For all compounds, FT‐Raman and two Vis spectra are presented along with the detailed band assignment. To the best of our knowledge, this is the first review showing the potential of Raman spectroscopy for the measurement and analysis of such a large collection of individual proteins. This work can serve as a comprehensive vibrational spectra library, based on our and previous Raman measurements. Copyright © 2013 John Wiley & Sons, Ltd.

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Section: Resultsmentioning

confidence: 99%

Raman spectroscopy of proteins: a review

Ryguła

Majzner

Marzec

et al. 2013

J Raman Spectroscopy

876

790

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“…102 UV-Raman has been used to investigate the protein structure of another phage. [107][108][109] Raman spectroscopy for toxin and chemical detection As a result of excitation at 257 nm, signals of the bases that build the genome were obtained, and characteristic Raman bands corresponding to the amino acids of the coat protein were attained as a result of excitation at 229 nm.…”

Section: Virusesmentioning

confidence: 99%

“…105 There have been several studies utilizing Raman spectroscopy for the investigation of Hepatitis viruses, but none of them have been reported as a foodborne virus. [107][108][109]…”

Section: Virusesmentioning

confidence: 99%

Dispersive and FT-Raman spectroscopic methods in food analysis

et al. 2015

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Raman spectroscopy is a powerful technique for molecular analysis of food samples. A fingerprint spectrum can be obtained for a target molecule by using Raman technology, as specific signals are obtained for chemical bonds in the target. In this way, food components, additives, processes and changes during shelf life, adulterations and numerous contaminants such as microorganisms, chemicals and toxins, can also be determined with or without the help of chemometric methods. The studies included in this review show that Raman spectroscopy has great potential for food analyses. In this review, we aim to bring together Raman studies on components, contaminants, raw materials, and adulterations of various food, and attempt to prepare a database of Raman bands obtained from food samples.

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“…The Raman spectra of tRNA at 30°C and 60°C are shown in Figure 3 a, where the peak at 810 cm −1 was assigned as the diester OPO stretching vibration (A-form marker), and the peak at 1098 cm −1 was assigned as the PO 2 − symmetric stretching vibration (inner reference, invariant to the base composition) 29 , 30 . In the aqueous solution of RNA polynucleotides, the peak value of the intensity ratio ( R : R = I 810 / I 1098 ) has been reported to vary from 0 to 1.64, depending on the percentage of nucleotide residue existing inside the segments of ordered structure of the A-form 31 - 33 . The R values obtained in the present study were 1.08 for 30°C and 0.87 for 60°C, showing that 66 % and 53 % of the A-form structure of the tRNA were maintained in these conditions.…”

Section: Resultsmentioning

confidence: 99%

Hydrophobic Properties of tRNA with Varied Conformations Evaluated by an Aqueous Two-Phase System

Suga¹,

Tomita²,

Tanaka³

et al. 2012

Int. J. Biol. Sci.

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The surface properties of transfer RNA (tRNA) were analyzed using a poly(ethylene glycol)/dextran aqueous two-phase system (ATPS), where the surface net hydrophobicity (HFS) and the local hydrophobicity (LH) were evaluated based on the partition coefficient of tRNA in the ATPS. According to the evaluated HFS values, the surface of the tRNA molecule was hydrophilic at 20° -40 °C, and it became hydrophobic at 50° -80 °C because of the exposure of the intrinsic nucleobases of tRNA. In contrast, the LH values were found to be maximal at 20° -40 °C. The conformation of tRNA was investigated by Raman and circular dichroism (CD) spectroscopies, corroborating the results with the calculated prediction of its secondary structure (Mfold). It was shown that 66% of A-form structure existed at room temperature; the base stacking (θ265) was gradually decreased, and the A-form structure (θ208) was denatured along with a sigmoid curve against the temperature increase; the denatured secondary structures were observed above 50° C by Mfold prediction. The HFS value of the DNA duplex was found to be hydrophilic, compared to that of the single-stranded DNA, indicating that the exposure of nucleobases is a key factor of the hydrophobic properties of nucleotides. We conclude that the hydrophobic property of the tRNA surface was directly affected by its conformational transition.

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Raman spectra and structure of a 25mer HCV RNA

Cited by 11 publications

References 36 publications

Raman spectroscopy of proteins: a review

Raman spectroscopy of proteins: a review

Dispersive and FT-Raman spectroscopic methods in food analysis

Hydrophobic Properties of tRNA with Varied Conformations Evaluated by an Aqueous Two-Phase System

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