On the stability of peptide secondary structures on the TiO<sub>2</sub> (101) anatase surface: a computational insight-Reference-Cited by-同舟云学术

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On the stability of peptide secondary structures on the TiO₂ (101) anatase surface: a computational insight

Published:2023 Issue:1 Volume:25 Page:392-401
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Pantaleone Stefano¹²^ORCID,Sodupe Mariona¹,Ugliengo Piero²^ORCID,Rimola Albert¹^ORCID

Affiliation:

1. Departament de Química, Universitat Autònoma de Barcelona, Bellaterra, 08193, Catalonia, Spain

2. Dipartimento di Chimica and Nanostructured Interfaces and Surfaces (NIS) Inter-Departmental Centre, Università degli Studi di Torino, Via P. Giuria 7, 10125, Torino, Italy

Abstract

The biological activity of proteins is partly due to their secondary structures and conformational states that may change in the presence of mineral surfaces.

Funder

Ministerio de Economía y Competitividad

Departament d'Innovació, Universitats i Empresa, Generalitat de Catalunya

Generalitat de Catalunya

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2023/CP/D2CP04395E

Reference68 articles.

1. Protein engineering

2. Protein engineering by chemical means?

3. Allosteric Changes in Protein Structure Computed by a Simple Mechanical Model: Hemoglobin T↔R2 Transition

4. 1.25 Å Resolution Crystal Structures of Human Haemoglobin in the Oxy, Deoxy and Carbonmonoxy Forms

5. Spectroscopic and Crystallographic Characterization of a Tetrameric Hemoglobin Oxidation Reveals Structural Features of the Functional Intermediate Relaxed/Tense State

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