Thermal broadening of Lb band of “trehalose coated” tyrosine and phenylalanine

Carrotta, Rita; Sanfratello, Vincenzo; Leone, Maurizio; Cordone, Lorenzo
April 2000
AIP Conference Proceedings;2000, Vol. 513 Issue 1, p83
Academic Journal
We studied the thermal broadening of Lb band of tyrosine and phenylalanine embedded in a trehalose matrix. Aim of this work is to obtain information on the effects of “trehalose coating” on the coupling of the electronic transition to low frequency modes in the surrounding of the chromophore. The results obtained for the two molecular complexes put in evidence that O-H groups are involved in blocking these structures within the solid trehalose matrix and shed light on the role played by hydrogen bonds on the interactions that keep “trehalose coated” proteins rigid and solid-like. © 2000 American Institute of Physics.


Related Articles

  • Enthalpic interaction between a-amino acids and pyridine and methylpyridine in aqueous solutions. Li, Y.; Xingen, H.; Ruisen, L.; Guiying, X. // Journal of Thermal Analysis & Calorimetry;2004, Vol. 76 Issue 2, p443 

    Enthalpies of dilution of aqueous L-serine, pyridine and methylpyridine solutions and their enthalpies of mixing have been determined by a mixing-flow microcalorimeter at 298.15 K. The data have been analyzed in terms of McMillan-Mayer formalism to fit to virial polynomials from which the...

  • Thermal studies on the sodium salts of aminosalicylic acids. Rotich, M. K.; Brown, M. E.; Glass, B. D. // Journal of Thermal Analysis & Calorimetry;2003, Vol. 73 Issue 2, p499 

    The effect on the stability of the isomers of aminosalicylic acid of formation of their sodium salts has been studied by use of differential scanning calorimetry and thermogravimetry, coupled with evolved gas analysis by Fourier transform infrared spectroscopy. X-ray powder diffraction and...

  • Excess molar heat capacities of ( L-glutamine aqueous solution+ D-glutamine aqueous solution) at temperatures between 293.15 and 303.15 K. Fujisawa, M.; Matsushita, T.; Khan, M. A.; Kimura, T. // Journal of Thermal Analysis & Calorimetry;Nov2005, Vol. 82 Issue 2, p319 

    Excess molar heat capacities of ( L-glutamine aqueous solution+ D-glutamine aqueous solution) were determined by using a differential scanning calorimeter at temperatures between 293.15 and 303.15 K. Excess molar heat capacities are all negative. Excess molar heat capacities decrease with...

  • Relation between chemical structure of amino acids and their thermal decomposition. Wesolowski, M.; Erecińska, J. // Journal of Thermal Analysis & Calorimetry;Nov2005, Vol. 82 Issue 2, p307 

    The influence of substituents on the thermal decomposition of monomeric organic compounds was studied. For this purpose the thermal destruction of dozen or so α-amino acids of the diversified chemical constitution, among others compounds containing the second amine group, additional carboxyl...

  • Two subsystems of meniscal collagen and their different thermal stabilities. Ignatieva, N.; Zakharkina, O.; Lunin, V.; Baratova, L.; Grokhovskaya, T.; Balalaeva, I.; Sergeeva, E. // Doklady Biochemistry & Biophysics;May2012, Vol. 444 Issue 1, p175 

    The article presents a study aims at determining a thermal stability of the collagen in meniscal tissue and clarifying its correlation with the functions of the organ. It notes that the amino acid analysis of hydrolysates of specimens and solutions has been conducted using a Hitachi-835 amino...

  • Differential Scanning Calorimetry of Light Meromyosin Fragments Having Various Lengths of Carp Fast Skeletal Muscle Isoforms1. Knkinuma, Makoto; Hatanaka, Akunasa; Fukushima, Hideto; Nakaya, Misako; Maeda, Kayo; Doi, Yukio; Ooi, Tatsuo; Watabe, Shugo // Journal of Biochemistry;2000, Vol. 128 Issue 1, p11 

    Various recombinant light meromyosin (LMM) fragments were prepared from cDNAs encoding the 10°C and 30°C types of myosin heavy chain isoforms predominantly expressed in fast skeletal muscles of the 10°C- and 30*C-acclimated carp, respectively. These included three kinds of quarter...

  • Thermal stability of amino acid-(tyrosine and tryptophan) coated magnetites. Patron, L.; Marinescu, G.; Culita, D.; Diamandescu, L.; Carp, O. // Journal of Thermal Analysis & Calorimetry;Feb2008, Vol. 91 Issue 2, p627 

    The thermal stability of two amino acid-(tyrosine and tryptophan) coated magnetite and their corresponding precursors, [FeFeII(Tyr)8]·9H2O and [FeFeII(Trp)2(OH)4](NO3)2·8H 2O (where tyrosine=Tyr and tryptophan=Trp), was analyzed in comparison with free amino acids. The complexes present a...

  • Effects of thermal history on solid state and melting behavior of amino acids. Matthews, M. Ellen; Riga, Alan T. // Journal of Thermal Analysis & Calorimetry;Jun2009, Vol. 96 Issue 3, p673 

    Dielectric Thermal Analysis (DETA) of drugs, proteins and amino acids reveals a strongly linear conductivity increase prior to and peaking at the melt, associated with dielectric viscoelastic properties of the material. Premelt onset and peak are shown to depend on thermal history. Comparisons...

  • Fingermark Detection on Thermal Papers: Proposition of an Updated Processing Sequence. Fitzi, Thomas; Fischer, Ruth; Moret, Sébastien; Bécue, Andy // Journal of Forensic Identification;2014, Vol. 64 Issue 4, p329 

    The detection of latent fingermarks on thermal papers proves to be particularly challenging because the application of conventional detection techniques may turn the sample dark grey or black, thus preventing the observation of fingermarks. Various approaches aiming at avoiding or solving this...


Read the Article


Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics