The unfolded- and folded-state infrared (IR) spectra of peptides studied to date show a common pattern, i.e., the amide I peak of the unfolded state is typically shifted toward higher frequencies with respect to the folded peak. Here, we study by means of a theoretical-computational method, the Perturbed Matrix Method (PMM), the IR spectra in the amide I region of two beta-hairpin peptides. The computed spectra are in good agreement with the experimental ones, thus providing an explanation of the physical origin underlying the differences of the unfolded- and folded-state spectra. (C) 2010 Elsevier B.V. All rights reserved.
On the origin of IR spectral changes upon protein folding / Isabella, Daidone; Massimiliano, Aschi; Laura Zanetti, Polzi; DI NOLA, Alfredo; Andrea, Amadei. - In: CHEMICAL PHYSICS LETTERS. - ISSN 0009-2614. - STAMPA. - 488:4-6(2010), pp. 213-218. [10.1016/j.cplett.2010.02.020]
On the origin of IR spectral changes upon protein folding
DI NOLA, Alfredo;
2010
Abstract
The unfolded- and folded-state infrared (IR) spectra of peptides studied to date show a common pattern, i.e., the amide I peak of the unfolded state is typically shifted toward higher frequencies with respect to the folded peak. Here, we study by means of a theoretical-computational method, the Perturbed Matrix Method (PMM), the IR spectra in the amide I region of two beta-hairpin peptides. The computed spectra are in good agreement with the experimental ones, thus providing an explanation of the physical origin underlying the differences of the unfolded- and folded-state spectra. (C) 2010 Elsevier B.V. All rights reserved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
