Potential of Raman spectroscopic techniques to study proteins

N Kuhar, S Sil, S Umapathy - Spectrochimica Acta Part A: Molecular and …, 2021 - Elsevier
Proteins are large, complex molecules responsible for various biological processes.
However, protein misfolding may lead to various life-threatening diseases. Therefore, it is …

A fresh look at the male-specific region of the human Y chromosome

Z Jangravi, M Alikhani, B Arefnezhad… - Journal of proteome …, 2013 - ACS Publications
The Chromosome-centric Human Proteome Project (C-HPP) aims to systematically map the
entire human proteome with the intent to enhance our understanding of human biology at …

Coordination to lanthanide ions distorts binding site conformation in calmodulin

SC Edington, A Gonzalez… - Proceedings of the …, 2018 - National Acad Sciences
The Ca2+-sensing protein calmodulin (CaM) is a popular model of biological ion binding
since it is both experimentally tractable and essential to survival in all eukaryotic cells. CaM …

[HTML][HTML] Novel microscale approaches for easy, rapid determination of protein stability in academic and commercial settings

CG Alexander, R Wanner, CM Johnson… - … et Biophysica Acta (BBA …, 2014 - Elsevier
Chemical denaturant titrations can be used to accurately determine protein stability.
However, data acquisition is typically labour intensive, has low throughput and is difficult to …

Raman spectra of amino acids and peptides from machine learning polarizabilities

E Berger, J Niemelä, O Lampela… - Journal of Chemical …, 2024 - ACS Publications
Raman spectroscopy is an important tool in the study of vibrational properties and
composition of molecules, peptides, and even proteins. Raman spectra can be simulated …

Interaction networks in protein folding via atomic-resolution experiments and long-time-scale molecular dynamics simulations

L Sborgi, A Verma, S Piana… - Journal of the …, 2015 - ACS Publications
The integration of atomic-resolution experimental and computational methods offers the
potential for elucidating key aspects of protein folding that are not revealed by either …

Application of millisecond time-resolved solid state NMR to the kinetics and mechanism of melittin self-assembly

J Jeon, KR Thurber, R Ghirlando… - Proceedings of the …, 2019 - National Acad Sciences
Common experimental approaches for characterizing structural conversion processes such
as protein folding and self-assembly do not report on all aspects of the evolution from an …

Ester carbonyl vibration as a sensitive probe of protein local electric field

IM Pazos, A Ghosh, MJ Tucker… - Angewandte Chemie …, 2014 - Wiley Online Library
The ability to quantify the local electrostatic environment of proteins and protein/peptide
assemblies is key to gaining a microscopic understanding of many biological interactions …

Using thioamides to site-specifically interrogate the dynamics of hydrogen bond formation in β-sheet folding

RM Culik, H Jo, WF DeGrado, F Gai - Journal of the American …, 2012 - ACS Publications
Thioamides are sterically almost identical to their oxoamide counterparts, but they are
weaker hydrogen bond acceptors. Therefore, thioamide amino acids are excellent …

Experimental validation of the role of trifluoroethanol as a nanocrowder

RM Culik, RM Abaskharon, IM Pazos… - The Journal of Physical …, 2014 - ACS Publications
Trifluoroethanol (TFE) is commonly used to induce protein secondary structure, especially α-
helix formation. Due to its amphiphilic nature, however, TFE can also self-associate to form …