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 …

Protein disulfide bond determination by mass spectrometry

JJ Gorman, TP Wallis, JJ Pitt - Mass spectrometry reviews, 2002 - Wiley Online Library
Abstract I. Introduction 184 II. Mass Spectrometry and Disulfide Bond Determination 185 A.
Peptide Mass Analysis 185 B. Peptide Mass Analysis for Determination of the Disulfides of …

Effect of reducing disulfide-containing proteins on electrospray ionization mass spectra

JA Loo, CG Edmonds, HR Udseth… - Analytical chemistry, 1990 - ACS Publications
(Arg, Lys, His), except for disulfide-containing molecules, such as lysozyme and bovine
albumin. However, reduction of disulfide linkages with 1, 4-dlthlothrelto)(Cleland's reagent) …

Characterization by tandem mass spectrometry of structural modifications in proteins

K Biemann, HA Scoble - Science, 1987 - science.org
Tandem mass spectrometry can be used to solve a number of protein structural problems
that are not amenable to conventional methods for amino acid sequencing. Typical …

Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP)

RA Williamson, FAO Marston, S Angal… - Biochemical …, 1990 - portlandpress.com
Disulphide bonds in human recombinant tissue inhibitor of metalloproteinases (TIMP) were
assigned by resolving proteolytic digests of TIMP on reverse-phase hplc and sequencing …

Formation of disulfide bonds in synthetic peptides and proteins

D Andreu, F Albericio, NA Solé, MC Munson… - Peptide synthesis …, 1995 - Springer
abstract Disulfide bridges play a crucial role in the folding and structural stabilization of
many important extracellular peptide and protein molecules, including hormones, enzymes …

Integration of mass spectrometry in analytical biotechnology

SA Carr, ME Hemling, MF Bean… - Analytical …, 1991 - ACS Publications
Mass spectrometry (MS) has become an Indispensable tool for peptide and protein structure
analysis because of three unique capabMties that enable It to beused to solve structural …

Identification and characterization of posttranslational modifications of proteins by MALDI ion trap mass spectrometry

J Qin, BT Chait - Analytical chemistry, 1997 - ACS Publications
Matrix-assisted laser desorption/ionization (MALDI) ion trap mass spectrometry is shown to
be a powerful tool for the elucidation of protein modifications. Low-energy covalent bonds …

[HTML][HTML] The human growth hormone receptor. Secretion from Escherichia coli and disulfide bonding pattern of the extracellular binding domain.

G Fuh, MG Mulkerrin, S Bass, N McFarland… - Journal of Biological …, 1990 - Elsevier
A gene fragment encoding the extracellular domain of the human growth hormone (hGH)
receptor from liver was cloned into a plasmid under control of the Escherichia coli alkaline …

Pro-sequence assisted folding and disulfide bond formation of human nerve growth factor

A Rattenholl, M Ruoppolo, A Flagiello, M Monti… - Journal of molecular …, 2001 - Elsevier
Nerve growth factor (NGF) is a member of the neurotrophin family. These growth factors
support neuronal survival and differentiation. Neurotrophins are synthesized as pre-pro …