2012
DOI: 10.1021/bi2018199
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Examining Protein Surface Structure in Highly Conserved Sequence Variants with Mass Spectrometry

Abstract: A simple mass spectrometry based method capable of examining protein structure called SNAPP (selective noncovalent adduct protein probing) is used to evaluate the structural consequences of point mutations in naturally occurring sequence variants from different species. SNAPP monitors changes in the attachment of noncovalent adducts to proteins as a function of structural state. Mutations which lead to perturbations to the electrostatic surface structure of a protein affect noncovalent attachment and are easil… Show more

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Cited by 7 publications
(6 citation statements)
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“…However, proton transfer significantly reduces the affinity of acidic groups for protonated amines (as are found in PE). However, hydrogen bond mediated noncovalent complexes between protonated primary amines and 18-crown-6 ether (18C6) are amenable to ESI-MS and have been utilized for a variety of experiments. …”
mentioning
confidence: 99%
“…However, proton transfer significantly reduces the affinity of acidic groups for protonated amines (as are found in PE). However, hydrogen bond mediated noncovalent complexes between protonated primary amines and 18-crown-6 ether (18C6) are amenable to ESI-MS and have been utilized for a variety of experiments. …”
mentioning
confidence: 99%
“…Several labeling-based strategies have been developed, including hydrogen–deuterium exchange (HDX), chemical cross-linking, , noncovalent labeling, and the use of chemical probes, ,, to characterize protein structures. Chemical probe strategies, ,, typically involve incubating a protein or protein complex with a reactive agent that covalently modifies exposed residues, thus allowing the development of a semiquantitative correlation between site-specific reactivity and solvent accessibility.…”
Section: Introductionmentioning
confidence: 99%
“…SNAPP is a comparative method that utilizes non-covalent attachment of probe molecules during ESI to monitor protein structure. SNAPP has been successfully used to reveal the effects of metal ions on the structure of α-synuclein [18], to monitor structural changes induced by single amino acid mutations [19], and to distinguish small structural differences in highly homologous proteins from different species [20]. 18-Crown-6 (18C6) is typically the probe molecule used in SNAPP experiments due to its ability to non-covalently bind to the protonated side chains of lysine and arginine, or to the N-terminus.…”
Section: Introductionmentioning
confidence: 99%