Infrared Spectrum of Matrix-Isolated Glycine

Grenié, Yves; Lassègues, J.C.; Garrigou‐Lagrange, C.

doi:10.1063/1.1674426

Cited by 63 publications

(33 citation statements)

References 11 publications

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“…Several examples prove that MI-IR spectroscopy is a powerful tool for studying the conformational landscape of biomolecules, including amino acid and small peptide models. The first MI-IR spectroscopic investigations on amino acid residues were performed by Grenie et al (1970), who studied glycine (Gly) in an Ar matrix. Since then Gly (Grenie and Garrigou-Lagrange1972; Reva et al 1995;Stepanian et al 1998a;Ivanov et al 1997Ivanov et al , 1999 Bazsó et al 2012a, b) and many other amino acids were thoroughly studied by MI-IR spectroscopy, including alanine (Rosado et al 1997;Stepanian et al 1998b;Lambie et al 2003;Bazsó et al 2013), valine (Stepanian et al 1999 Our present aim is to determine the conformational distribution of (ACBA) derivatives by MI-IR spectroscopy and to show that the local chirality of the building block fully controls their folding preferences.…”

Section: Introductionmentioning

confidence: 99%

“…Several examples prove that MI-IR spectroscopy is a powerful tool for studying the conformational landscape of biomolecules, including amino acid and small peptide models. The first MI-IR spectroscopic investigations on amino acid residues were performed by Grenie et al (1970), who studied glycine (Gly) in an Ar matrix. Since then Gly (Grenie and Garrigou-Lagrange1972;Reva et al 1995;Stepanian et al 1998a;Ivanov et al 1997Ivanov et al , 1999Bazsó et al 2012a, b) and many other amino acids were thoroughly studied by MI-IR spectroscopy, including alanine (Rosado et al 1997;Stepanian et al 1998b;Lambie et al 2003;Bazsó et al 2013), valine (Stepanian et al 1999), leucine (Sheina et al 1988), isoleucine (Boeckx and Maes 2012a), proline (Reva et al 1994;Stepanian et al 2001), serine (Lambie et al 2004;Jarmelo et al 2005;Jarmelo et al 2006), phenylalanine (Kaczor et al 2006), tyrosine (Ramaekers et al 2005), tryptophan (Kaczor et al 2007), cysteine (Dobrowolski et al 2007), asparagine (Boeckx and Maes 2012b), lysine (Boeckx and Maes 2012c), and β-alanine (Rosado et al 1997;Dobrowolski et al 2008).…”

Section: Introductionmentioning

confidence: 99%

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Foldamers of β-peptides: conformational preference of peptides formed by rigid building blocks. The first MI-IR spectra of a triamide nanosystem

et al. 2013

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IntroductionAlthough dynamic on a large timescale of motion, some biologically active polyamide nanosystems adopt welldefined 3D structures in a time average manner, called as globular proteins; a given name reflecting to their overall shape. Other proteins called intrinsically unstructured or dynamic (IUP or IDP) are reluctant to present such an easy to characterize structural ensemble, nicknamed as proteins with random structures. Thus, proteins exist in most phases as conformational ensembles presenting lower, while in other environment higher time average deviation from their average 3D folds. The α-amino acid sequence modification of these inherently dynamic polyamide systems can lower, or increase the amplitude and frequency of such internal motion, making the protein fold less or more -mobile‖. The chemical constitution (α) and the stereochemistry (L) of proteogenic amino acid residues are under strict evolutional conservation. Unlike L-Proline, all the remaining 19 common residues in proteins have two adjacent backbone torsional angles, φ and ψ, of high rotational freedom followed by the inflexible ω. The scenario of two flexible followed by a fixed backbone torsional angles per residue determines primarily the folding ability of a proteogenic polypeptide. Cutting of a globular fold seldom results in secondary structural elements (e.g. α-helix, β-turn) of low internal dynamics! Typically the removal of any secondary structural element from its -natural environment‖ results in polypetides of very elevated internal dynamics, often characterized as unstructured subunits. However, bioengineering requires stable toolkits to design epitopes, matching complementary folds, individual foldamers, nano-lego elements etc. of traceable shape and of low internal mobility. Shedding light on folding and stability of secondary structural elements of peptides and proteins could help to design standalone foldamers. They could be composed of β-, α-and α/β-amino acid residues, the latter called chimera. A general expectation of foldamers is to present a single time average 3D-structure of lower internal dynamics over the large timescale of picoseconds to second. These fold optimized biocompatible and nonnatural peptides often have an increased proteolytic and metabolic stability and can fulfill diverse biological functions toward DNA, RNA, ATP, etc. The improved ability of β-peptides and thus β-foldamers to rapidly and spontaneously fold (

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Section: Introductionmentioning

confidence: 99%

“…Several examples prove that MI-IR spectroscopy is a powerful tool for studying the conformational landscape of biomolecules, including amino acid and small peptide models. The first MI-IR spectroscopic investigations on amino acid residues were performed by Grenie et al (1970), who studied glycine (Gly) in an Ar matrix. Since then Gly (Grenie and Garrigou-Lagrange1972;Reva et al 1995;Stepanian et al 1998a;Ivanov et al 1997Ivanov et al , 1999Bazsó et al 2012a, b) and many other amino acids were thoroughly studied by MI-IR spectroscopy, including alanine (Rosado et al 1997;Stepanian et al 1998b;Lambie et al 2003;Bazsó et al 2013), valine (Stepanian et al 1999), leucine (Sheina et al 1988), isoleucine (Boeckx and Maes 2012a), proline (Reva et al 1994;Stepanian et al 2001), serine (Lambie et al 2004;Jarmelo et al 2005;Jarmelo et al 2006), phenylalanine (Kaczor et al 2006), tyrosine (Ramaekers et al 2005), tryptophan (Kaczor et al 2007), cysteine (Dobrowolski et al 2007), asparagine (Boeckx and Maes 2012b), lysine (Boeckx and Maes 2012c), and β-alanine (Rosado et al 1997;Dobrowolski et al 2008).…”

Section: Introductionmentioning

confidence: 99%

Foldamers of β-peptides: conformational preference of peptides formed by rigid building blocks. The first MI-IR spectra of a triamide nanosystem

et al. 2013

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“…[1][2][3] Amino acids adopt their neutral form also in the gas phase [4][5][6][7][8][9][10][11][12][13] and in low-temperature inert matrixes. [14][15][16][17][18][19][20][21][22][23][24][25][26][27][28] Therefore, the structures of these compounds have been extensively studied in both these media. A number of aliphatic amino acids as well as some of their derivatives have been investigated experimentally up to date: glycine, 4,5,[14][15][16][17][18] sarcosine (N-methylglycine), 19 N,N-dimethylglycine, 20 alanine, 6,[21][22][23] valine, 7,24 proline 8,25,26 and serine.…”

Section: Introductionmentioning

confidence: 99%

“…[14][15][16][17][18][19][20][21][22][23][24][25][26][27][28] Therefore, the structures of these compounds have been extensively studied in both these media. A number of aliphatic amino acids as well as some of their derivatives have been investigated experimentally up to date: glycine, 4,5,[14][15][16][17][18] sarcosine (N-methylglycine), 19 N,N-dimethylglycine, 20 alanine, 6,[21][22][23] valine, 7,24 proline 8,25,26 and serine. 27,28 Most of these studies also reported theoretical calculations at various levels of theory.…”

Section: Introductionmentioning

confidence: 99%

Importance of Entropy in the Conformational Equilibrium of Phenylalanine: A Matrix-Isolation Infrared Spectroscopy and Density Functional Theory Study

et al. 2006

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The conformational behavior and infrared spectrum of L-phenylalanine were studied by matrix-isolation infrared spectroscopy and DFT [B3LYP/6-311++G(d,p)] calculations. The fourteen most stable structures were predicted to differ in energy by less than 10 kJ mol -1 , eight of them with abundances higher than 5% at the temperature of evaporation of the compound (423 K). Experimental results suggest that six conformers contribute to the spectrum of the isolated compound, whereas two conformers (IIb 3 and IIIb 3 ) relax in matrix to a more stable form (IIb 2 ) due to low energy barriers for conformational isomerization (conformational cooling). The two lowest-energy conformers (Ib 1 , Ia) differ only in the arrangement of the amino acid group relative to the phenyl ring; they exhibit a relatively strong stabilizing intramolecular hydrogen bond of the O-H‚‚‚N type and the carboxylic group in the trans configuration (OdC-O-H dihedral angle ca. 180°). Type II conformers have a weaker H-bond of the N-H‚‚‚OdC type, but they bear the more favorable cis arrangement of the carboxylic group. Being considerably more flexible, type II conformers are stabilized by entropy and the relative abundances of two conformers of this type (IIb 2 and IIc 1 ) are shown to significantly increase with temperature due to entropic stabilization. At 423 K, these conformers are found to be the first and third most abundant species present in the conformational equilibrium, with relative populations of ca. 15% each, whereas their populations could be expected to be only ca. 5% if entropy effects were not taken into consideration. Indeed, phenylalanine can be considered a notable example of a molecule where entropy plays an essential role in determining the relative abundance of the possible low-energy conformational states and then, the thermodynamics of the compound, even at moderate temperatures. Upon UV irradiation (λ > 235 nm) of the matrix-isolated compound, unimolecular photodecomposition of phenylalanine is observed with production of CO 2 and phenethylamine.

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“…It is believed that amino acids usually exist in their zwitterionic forms in aqueous solution within a certain range of pH. However, whether the zwitterions can exist in gas phase has been extensively discussed [5][6][7][8][9][10][11][12][13][14][15][16][17]. Normally, the zwitterionic charge separation needs to be stabilized by the environment.…”

Section: Introductionmentioning

confidence: 99%

The role of dimerization on the structure transformation of arginine in gas phase

Lin

Luo

2014

Chemical Physics Letters

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Infrared Spectrum of Matrix-Isolated Glycine

Cited by 63 publications

References 11 publications

Foldamers of β-peptides: conformational preference of peptides formed by rigid building blocks. The first MI-IR spectra of a triamide nanosystem

Foldamers of β-peptides: conformational preference of peptides formed by rigid building blocks. The first MI-IR spectra of a triamide nanosystem

Importance of Entropy in the Conformational Equilibrium of Phenylalanine: A Matrix-Isolation Infrared Spectroscopy and Density Functional Theory Study

The role of dimerization on the structure transformation of arginine in gas phase

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