Mass spectrometry-based protein footprinting for higher-order structure analysis: fundamentals and applications

XR Liu, MM Zhang, ML Gross - Chemical reviews, 2020 - ACS Publications
Proteins adopt different higher-order structures (HOS) to enable their unique biological
functions. Understanding the complexities of protein higher-order structures and dynamics …

Role of the molten globule state in protein folding

M Arai, K Kuwajima - Advances in protein chemistry, 2000 - Elsevier
Publisher Summary This chapter deals with the structure of the molten globules of various
globular proteins revealed by the recent experimental studies. Recent advances in …

Forced unfolding of proteins within cells

CP Johnson, HY Tang, C Carag, DW Speicher… - Science, 2007 - science.org
To identify cytoskeletal proteins that change conformation or assembly within stressed cells,
in situ labeling of sterically shielded cysteines with fluorophores was analyzed by …

Detection of multiple protein conformational ensembles in solution via deconvolution of charge-state distributions in ESI MS

A Dobo, IA Kaltashov - Analytical chemistry, 2001 - ACS Publications
Monitoring the changes in charge-state distributions of protein ions in electrospray ionization
(ESI) mass spectra has become one of the commonly accepted tools to detect large-scale …

Protein‐folding kinetics and mechanisms studied by pulse‐labeling and mass spectrometry

L Konermann, DA Simmons - Mass spectrometry reviews, 2003 - Wiley Online Library
Abstract I. Introduction 2 A. The Protein‐Folding Problem 2 B. Protein‐Folding Mechanisms
3 C. The Role of Folding Intermediates 3 II. Studies on Protein‐Folding Intermediates by …

Kinetic evidence for a two-stage mechanism of protein denaturation by guanidinium chloride

SK Jha, S Marqusee - … of the National Academy of Sciences, 2014 - National Acad Sciences
Dry molten globular (DMG) intermediates, an expanded form of the native protein with a dry
core, have been observed during denaturant-induced unfolding of many proteins. These …

Single-molecule covalent chemistry with spatially separated reactants

T Luchian, SH Shin, H Bayley - … (International ed. in …, 2003 - pubmed.ncbi.nlm.nih.gov
Single-molecule covalent chemistry with spatially separated reactants Single-molecule covalent
chemistry with spatially separated reactants Angew Chem Int Ed Engl. 2003 Aug 18;42(32):3766-71 …

[HTML][HTML] Thermodynamics of co-translational folding and ribosome–nascent chain interactions

CA Waudby, C Burridge, LD Cabrita… - Current Opinion in …, 2022 - Elsevier
Proteins can begin the conformational search for their native structure in parallel with
biosynthesis on the ribosome, in a process termed co-translational folding. In contrast to the …

Dynamics of equilibrium structural fluctuations of apomyoglobin measured by fluorescence correlation spectroscopy

H Chen, E Rhoades, JS Butler… - Proceedings of the …, 2007 - National Acad Sciences
The spectra of equilibrium chain conformation fluctuations of apomyoglobin (apoMb) as a
function of folding, from the acid-denatured state at pH 2.6 through the stable molten globule …

Site‐specific Heterogeneity of Multi‐domain Human Serum Albumin and its Origin: A Red Edge Excitation Shift Study

N Das, S Sahu, T Khan, P Sen - Photochemistry and …, 2023 - Wiley Online Library
Conformational heterogeneity is a defining characteristic of a protein and is vital in
understanding its function and folding landscape. In the present work, we interrogated the …