Abstract:The ir and Raman spectra of α and β‐DL‐methionine and three isotopomers have been recorded and assigned with the help of normal coordinate analyses. The vibrational intensities of three conformers (χ1 = gauche II; χ2 = trans; χ3 = gauche I, trans, and gauche II) have been calculated for the free molecule with a MNDO program including a finite field perturbation. Except for the vibrations including the S atom, the CO−2 and NH+3 group the calculations agree with experimental data and confirm the change of χ3 fro… Show more
“…The first ratio is assumed to be sensitive to lateral chain−chain interactions and the second ratio is sensitive to intermolecular interactions, but also it should reflect the mobility of the methyl terminal group of hydrocarbon chains. Thus, the lower the intensity ratio is, the higher the conformational order of the alkyl chain and the lower mobility of the methyl end group is obtained. ,, Figure represents the changes in Raman peak height intensity ratios in relation to temperature of dl -norvaline. It is shown clearly that there are two temperature regions at about −120 and −76 °C, in which an increase of the intensity ratios is observed that almost corresponds to the phase transitions observed by DSC.…”
Section: Resultsmentioning
confidence: 99%
“…This table summarizes conformationally sensitive bands which are showed differences during phase transition and will be discussed in the text. Bands were assigned by comparison with similar compounds. ,,,,,,− ,, …”
Section: Resultsmentioning
confidence: 99%
“…The structural variations in the solid state constitute a simple model for conformational dependence in biochemical processes. In particular, the thermal analysis on solid−solid phase transitions between crystalline amino acids brings suggestive information on transition phenomena of biological systems, especially of biomembranes. − …”
The structural modifications of the amino acid DL-Norvaline have been studied using differential scanning calorimetry (DSC) and Raman spectroscopy. DSC results showed that this amino acid undergoes two solid-solid phase transitions at -116.9 and -76.1 degrees C in the temperature range -130 to +300 degrees C. Raman spectroscopy was applied to complement DSC results. The combination of the two methodologies point out that the observed phase transitions correspond to an increment of disordering in the aliphatic side chain of amino acid, an augmentation of the rotational motion of the amino group and a decrease of the strength of the intramolecular hydrogen bonding of the initial dimers at low temperatures. The observed phase transitions of DL-norvaline are compared with those found in DL-norleucine.
“…The first ratio is assumed to be sensitive to lateral chain−chain interactions and the second ratio is sensitive to intermolecular interactions, but also it should reflect the mobility of the methyl terminal group of hydrocarbon chains. Thus, the lower the intensity ratio is, the higher the conformational order of the alkyl chain and the lower mobility of the methyl end group is obtained. ,, Figure represents the changes in Raman peak height intensity ratios in relation to temperature of dl -norvaline. It is shown clearly that there are two temperature regions at about −120 and −76 °C, in which an increase of the intensity ratios is observed that almost corresponds to the phase transitions observed by DSC.…”
Section: Resultsmentioning
confidence: 99%
“…This table summarizes conformationally sensitive bands which are showed differences during phase transition and will be discussed in the text. Bands were assigned by comparison with similar compounds. ,,,,,,− ,, …”
Section: Resultsmentioning
confidence: 99%
“…The structural variations in the solid state constitute a simple model for conformational dependence in biochemical processes. In particular, the thermal analysis on solid−solid phase transitions between crystalline amino acids brings suggestive information on transition phenomena of biological systems, especially of biomembranes. − …”
The structural modifications of the amino acid DL-Norvaline have been studied using differential scanning calorimetry (DSC) and Raman spectroscopy. DSC results showed that this amino acid undergoes two solid-solid phase transitions at -116.9 and -76.1 degrees C in the temperature range -130 to +300 degrees C. Raman spectroscopy was applied to complement DSC results. The combination of the two methodologies point out that the observed phase transitions correspond to an increment of disordering in the aliphatic side chain of amino acid, an augmentation of the rotational motion of the amino group and a decrease of the strength of the intramolecular hydrogen bonding of the initial dimers at low temperatures. The observed phase transitions of DL-norvaline are compared with those found in DL-norleucine.
“…Figs. 3(a) and (b) show CH 3 -S stretching region and -COO-vibration region, respectively [2]. The spectra observed at 333 K are different from others, indicating that the structural change of the crystal occurred between 323 and 333 K.…”
“…Earlier infrared studies of methionine and selenomethionine, which utilized solid-state amino acids (Shepherd and Huber, 1969;Tamba et al, 1973), revealed that the S!Se substitution had a small effect on the 1800-1400 cm ÿ1 region but altered many peaks below 1400 cm ÿ1 . The latter bands represent various vibrational modes of the methionine side chain and typically have medium intensity (Grunenberg and Bougeard, 1986). Because our difference spectra exhibited only two bands at 1284 and 903/899 cm ÿ1 , which are sensitive to the S!Se replacement, it appears that only minor alterations of the chemical bonds involving sulfur occur during the BR!M transition.…”
Bacteriorhodopsin (BR) is an integral membrane protein, which functions as a light-driven proton pump in Halobacterium salinarum. We report evidence that one or more methionine residues undergo a structural change during the BR-->M portion of the BR photocycle. Selenomethionine was incorporated into BR using a cell-free protein translation system containing an amino acid mixture with selenomethionine substituted for methionine. BR-->M FTIR difference spectra recorded for unlabeled and selenomethionine-labeled cell-free expressed BR closely resemble the spectra of in vivo expressed BR. However, reproducible changes occur in two regions near 1,284 and 900 cm(-1) due to selenomethionine incorporation. Isotope labeled tyrosine was also co-incorporated with selenomethionine in order to confirm these assignments. Based on recent x-ray crystallographic studies, likely methionines which give rise to the FTIR difference bands are Met-118 and Met-145, which are located inside the retinal binding pocket and in a position to constrain the motion of retinal during photoisomerization. The assignment of methionine bands in the FTIR difference spectrum of BR provides a means to study methionine-chromophore interaction under physiological conditions. More generally, combining cell-free incorporations of selenomethionine into proteins with FTIR difference spectroscopy provides a useful method for investigating the role of methionines in protein structure and function.
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