Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases

L Whitmore, BA Wallace - Biopolymers: Original Research on …, 2008 - Wiley Online Library
Circular dichroism (CD) spectroscopy has been a valuable method for the analysis of protein
secondary structures for many years. With the advent of synchrotron radiation circular …

CAPITO—a web server-based analysis and plotting tool for circular dichroism data

C Wiedemann, P Bellstedt, M Görlach - Bioinformatics, 2013 - academic.oup.com
Motivation: Circular dichroism (CD) spectroscopy is one of the most versatile tools to study
protein folding and to validate the proper fold of purified proteins. Here, we aim to provide a …

[PDF][PDF] The use of circular dichroism spectroscopy to study protein folding, form and function

DHA Corrêa, CHI Ramos - African Journal of Biochemistry …, 2009 - researchgate.net
Circular Dichroism (CD) is a spectroscopic technique widely used for the evaluation of the
conformation and stability of proteins in several environmental conditions like temperature …

Evaluation of the information content in infrared spectra for protein secondary structure determination

E Goormaghtigh, JM Ruysschaert, V Raussens - Biophysical journal, 2006 - cell.com
Fourier-transform infrared spectroscopy is a method of choice for the experimental
determination of protein secondary structure. Numerous approaches have been developed …

Protein adsorption onto nanoparticles induces conformational changes: Particle size dependency, kinetics, and mechanisms

P Satzer, F Svec, G Sekot… - Engineering in life …, 2016 - Wiley Online Library
The use of nanomaterials in bioapplications demands a detailed understanding of protein–
nanoparticle interactions. Proteins can undergo conformational changes while adsorbing …

Evolutionary conservation of biogenesis of β-barrel membrane proteins

SA Paschen, T Waizenegger, T Stan, M Preuss… - Nature, 2003 - nature.com
The outer membranes of mitochondria and chloroplasts are distinguished by the presence of
β-barrel membrane proteins,. The outer membrane of Gram-negative bacteria also harbours …

Biophysical methods to investigate intrinsically disordered proteins: avoiding an “elephant and blind men” situation

VN Uversky - Intrinsically Disordered Proteins Studied by NMR …, 2015 - Springer
Intrinsically disordered proteins (IDPs) and hybrid proteins possessing ordered domains and
intrinsically disordered protein regions (IDPRs) are highly abundant in various proteomes …

Acidosis-induced activation of anion channel SLAH3 in the flooding-related stress response of Arabidopsis

J Lehmann, ME Jørgensen, S Fratz, HM Müller… - Current Biology, 2021 - cell.com
Plants, as sessile organisms, gained the ability to sense and respond to biotic and abiotic
stressors to survive severe changes in their environments. The change in our climate comes …

Komodo dragon-inspired synthetic peptide DRGN-1 promotes wound-healing of a mixed-biofilm infected wound

EMC Chung, SN Dean, CN Propst, BM Bishop… - npj Biofilms and …, 2017 - nature.com
Cationic antimicrobial peptides are multifunctional molecules that have a high potential as
therapeutic agents. We have identified a histone H1-derived peptide from the Komodo …

Constructing a photo-enzymatic cascade reaction and its in situ monitoring: enzymes hierarchically trapped in titania meso-porous MOFs as a new photosynthesis …

J Guo, L Yang, C Zhao, Z Gao, YY Song… - Journal of Materials …, 2021 - pubs.rsc.org
A photocatalysis-enzyme coupled system represents a most promising approach towards
artificial photosynthesis and a direct use of solar energy for the synthesis of specific organic …