Accessibility governs the relative reactivity of basic residues in formaldehyde-induced protein modifications

Analytica Chimica Acta

Volumn 676, Issue 1-2, 2010, Pages 60-67

  Toews, Judy ^a   Rogalski, Jason C ^a   Kast, Juergen ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

Chemical modification; Formaldehyde; Mass spectrometry; Peptide fragmentation; Protein cross linking; Reactivity; Residue accessibility

Indexed keywords

COVALENT LINK; FOLDED PROTEINS; IN-VIVO; INDUCED PROTEINS; MILD REACTION CONDITIONS; MODEL PROTEINS; MODEL STUDY; PEPTIDE FRAGMENTATION; PROTEIN CROSS-LINKING; REACTIVE INTERMEDIATE; REACTIVITY; RELATIVE REACTIVITIES; RESIDUE ACCESSIBILITY; SOLVENT ACCESSIBLE SURFACE AREAS; STRUCTURAL STABILITIES; TERTIARY STRUCTURES;

AMINO ACIDS; CELL MEMBRANES; CYTOLOGY; FORMALDEHYDE; MASS SPECTROMETRY; PEPTIDES; REACTION INTERMEDIATES; STABILITY; SURFACE STRUCTURE;

CHEMICAL MODIFICATION;

AMINE; FORMALDEHYDE; LYSINE; PEPTIDE; SCHIFF BASE;

ARTICLE; CELL MEMBRANE PERMEABILITY; CHEMICAL MODIFICATION; CHEMICAL REACTION; CONTROLLED STUDY; COVALENT BOND; IN VIVO STUDY; MICROENVIRONMENT; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN FOLDING; PROTEIN MODIFICATION; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SEQUENCE; CROSS-LINKING REAGENTS; FORMALDEHYDE; MYOGLOBIN; PROTEIN STRUCTURE, TERTIARY; PROTEINS; SERINE ENDOPEPTIDASES; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 77956173802     PISSN: 00032670     EISSN: 18734324     Source Type: Journal    
DOI: 10.1016/j.aca.2010.07.040     Document Type: Article

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