Conformational control of cofactors in nature–the influence of protein-induced macrocycle distortion on the biological function of tetrapyrroles

MO Senge, SA MacGowan, JM O'Brien - Chemical Communications, 2015 - pubs.rsc.org
Tetrapyrrole-containing proteins are one of the most fundamental classes of enzymes in
nature and it remains an open question to give a chemical rationale for the multitude of …

Origin of the red shifts in the optical absorption bands of nonplanar tetraalkylporphyrins

RE Haddad, S Gazeau, J Pécaut… - Journal of the …, 2003 - ACS Publications
The view that the large red shifts seen in the UV− visible absorption bands of peripherally
crowded nonplanar porphyrins are the result of nonplanar deformations of the macrocycle …

Sterically induced distortions of nickel (II) porphyrins–Comprehensive investigation by DFT calculations and resonance Raman spectroscopy

J Schindler, S Kupfer, AA Ryan, KJ Flanagan… - Coordination Chemistry …, 2018 - Elsevier
Abstract A series of 5, 15-disubstituted and 5, 10, 15, 20-tetrasubstituted, and 5, 10, 15, 20-
tetrasubstituted-2, 3, 7, 8, 12, 13, 17, 18-octaethyl nickel (II) porphyrins in dichloromethane is …

[HTML][HTML] Heme–protein interactions and functional relevant heme deformations: the cytochrome c case

R Schweitzer-Stenner - Molecules, 2022 - mdpi.com
Heme proteins are known to perform a plethora of biologically important functions. This
article reviews work that has been conducted on various class I cytochrome c proteins over a …

Tripeptides adopt stable structures in water. A combined polarized visible Raman, FTIR, and VCD spectroscopy study

F Eker, X Cao, L Nafie… - Journal of the American …, 2002 - ACS Publications
We have measured the band profile of amide I in the infrared, isotropic, and anisotropic
Raman spectra of L-alanyl-D-alanyl-L-alanine, acetyl-L-alanyl-L-alanine, L-vanyl-L-vanyl-L …

Intrinsic propensities of amino acid residues in GxG peptides inferred from amide I′ band profiles and NMR scalar coupling constants

A Hagarman, TJ Measey, D Mathieu… - Journal of the …, 2010 - ACS Publications
A reliable intrinsic propensity scale of amino acid residues is indispensable for an
assessment of how local conformational distributions in the unfolded state can affect the …

The conformation of tetraalanine in water determined by polarized Raman, FT-IR, and VCD spectroscopy

R Schweitzer-Stenner, F Eker… - Journal of the …, 2004 - ACS Publications
The present article reports the conformation of cationic tetraalanine in aqueous solution. The
determination of the dihedral angles of the two central amino acid residues was achieved by …

Dihedral Angles of Trialanine in D2O Determined by Combining FTIR and Polarized Visible Raman Spectroscopy

R Schweitzer-Stenner, F Eker, Q Huang… - Journal of the …, 2001 - ACS Publications
We have measured the polarized visible Raman and FTIR spectra of trialanine and triglycine
in D2O at acid, neutral, and alkaline pD. From the Raman spectra we obtained the isotropic …

Preferred peptide backbone conformations in the unfolded state revealed by the structure analysis of alanine-based (AXA) tripeptides in aqueous solution

F Eker, K Griebenow, X Cao, LA Nafie… - Proceedings of the …, 2004 - pnas.org
We have combined Fourier transform IR, polarized Raman spectroscopy, and vibrational CD
measurements of the amide I′ band profile of alanyl-X-alanine tripeptides in 2H2O to …

Perturbation of water structure by water-polymer interactions probed by FTIR and polarized Raman spectroscopy

J Pavelec, D DiGuiseppi, BY Zavlavsky… - Journal of Molecular …, 2019 - Elsevier
Infrared and polarized Raman spectroscopy are ideal tools to probe changes of water
structure caused by the addition of water soluble polymers. In this paper, we investigate how …