Visible and UV‐resonance Raman spectroscopy of model peptides

Schweitzer‐Stenner, Reinhard

doi:10.1002/jrs.757

Cited by 73 publications

(64 citation statements)

References 94 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…transitions in the xy-plane of the peptide group. 5 A weak z-component can be brought about either by coupling to the charge-transfer transitions n COO ! peptide and COO !…”

Section: Conceptsmentioning

confidence: 99%

“…1 -4 The corresponding normal mode of the peptide linkage is predominately a CO stretching vibration with some admixture from NH in-plane bending, CN stretching and C˛(C)H in-plane bending. 1,5 Amide I modes of adjacent peptide groups can interact by through-bond and throughspace coupling. 1,6,7 This gives rise to delocalized, excitonic vibrational states.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Conformational analysis of tetrapeptides by exploiting the excitonic coupling between amide I modes

Huang

Schweitzer‐Stenner

2004

J Raman Spectroscopy

Self Cite

View full text Add to dashboard Cite

The amide I band of the IR and to a lesser extent also of the corresponding visible Raman spectra of peptides and proteins are frequently used to determine their secondary structure composition. Thus far, however, this analytical approach is generally a low-resolution technique, particularly because it mostly discriminates only between a-helical, b-sheet (parallel and antiparallel) and so-called random coil conformations. This study shows that for tetrapeptides the combined use of the IR and Raman amide I band profiles allows one to discriminate currently known secondary structure motifs. To exploit the spectral information to its fullest extent, we developed an algorithm which calculates the amide I intensity profiles of IR, isotropic and anisotropic Raman scattering and also the depolarization ratios of the Raman bands as a function of the dihedral angles of the two central amino acid resides. The approach is based on a quantum mechanical treatment of the vibrational coupling between the amide I modes of the three peptide groups in the framework of a coupled oscillator model. We calculated the band profiles of a representative set of secondary structures, i.e. a right-handed a-helix, a 3 10 -helix, b-sheets and a polyproline II (PPII)-type 3 1 -helix and b-turns. Our results unambiguously show that all these secondary structure motifs can be identified by comparing experimentally observed IR and Raman amide I bands with their respective calculated intensity distributions.

show abstract

“…transitions in the xy-plane of the peptide group. 5 A weak z-component can be brought about either by coupling to the charge-transfer transitions n COO ! peptide and COO !…”

Section: Conceptsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Conformational analysis of tetrapeptides by exploiting the excitonic coupling between amide I modes

Huang

Schweitzer‐Stenner

2004

J Raman Spectroscopy

Self Cite

View full text Add to dashboard Cite

show abstract

“…Keywords: ab initio calculations · chirality · helical structures · protein structures · vibrational spectroscopy over two frequency axes such as two-dimensional IR spectroscopy, [5,[9][10][11][12] or that filter specific spectroscopic information such as resonance Raman spectroscopy [13][14][15][16][17] often provide more detailed information on the secondary structure of polypeptides and proteins. Similarly, chiral vibrational spectroscopy filters out information related to the chirality of the investigated molecule.…”

Section: Introductionmentioning

confidence: 99%

Understanding the Signatures of Secondary‐Structure Elements in Proteins with Raman Optical Activity Spectroscopy

Jacob

Luber

Reiher

2009

Chemistry A European J

110

View full text Add to dashboard Cite

A prerequisite for the understanding of functional molecules like proteins is the elucidation of their structure under reaction conditions. Chiral vibrational spectroscopy is one option for this purpose, but provides only indirect access to this structural information. By first-principles calculations, we investigate how Raman optical activity (ROA) signals in proteins are generated and how signatures of specific secondary-structure elements arise. As a first target we focus on helical motifs and consider polypeptides consisting of twenty alanine residues to represent alpha-helical and 3(10)-helical secondary-structure elements. Although ROA calculations on such large molecules have not been carried out before, our main goal is the stepwise reconstruction of the ROA signals. By analyzing the calculated ROA spectra in terms of rigorously defined localized vibrations, we investigate in detail how total band intensities and band shapes emerge. We find that the total band intensities can be understood in terms of the reconstructed localized vibrations on individual amino acid residues. Two different basic mechanisms determining the total band intensities can be established, and it is explained how structural changes affect the total band intensities. The band shapes can be rationalized in terms of the coupling between the localized vibrations on different residues, and we show how different band shapes arise as a consequence of different coupling patterns. As a result, it is demonstrated for the chiral variant of Raman spectroscopy how collective vibrations in proteins can be understood in terms of well-defined localized vibrations. Based on our calculations, we extract characteristic ROA signatures of alpha helices and of 3(10)-helices, which our analysis directly relates to differences in secondary structure.

show abstract

“…Therefore, these two modes have been the maker band for detecting the secondary structure of polypeptides and proteins. 30,31 Figure 2(a) shows Raman spectra of the skeletal stretching mode of AAlaMA in aqueous solution. The four peaks of 842, 859, 885, and 924 cm Ϫ1 were determined by the second derivative analysis of the original spectra.…”

mentioning

confidence: 99%

Temperature and pressure effects on conformational equilibria of alanine dipeptide in aqueous solution

et al. 2004

View full text Add to dashboard Cite

We investigated the temperature and pressure effects on conformational equilibria of N-acetyl-L-alanine-N'-methylamide (AAlaMA) in aqueous solution by Raman spectroscopy. Scattering intensities in the skeletal stretching mode of AAlaMA in aqueous solution were decomposed into some component bands by the spectra analysis. Our results indicate that each component band for AAlaMA adopts not only the P(II) and alpha(R) conformations but also the C(7eq) conformation. From temperature and pressure dependencies of the band intensities, we determined the enthalpy differences and the volume differences between the conformers. The C(7eq) conformer is enthalpically most stable due to the intramolecular hydrogen bond. The partial molar volume of the C(7eq) conformer is the smallest through the solvent-exclusion effect rather than the solute-solvent electrostatic interaction effect.

show abstract

Visible and UV‐resonance Raman spectroscopy of model peptides

Cited by 73 publications

References 94 publications

Conformational analysis of tetrapeptides by exploiting the excitonic coupling between amide I modes

Conformational analysis of tetrapeptides by exploiting the excitonic coupling between amide I modes

Understanding the Signatures of Secondary‐Structure Elements in Proteins with Raman Optical Activity Spectroscopy

Temperature and pressure effects on conformational equilibria of alanine dipeptide in aqueous solution

Contact Info

Product

Resources

About