Works (2)

Updated: July 5th, 2023 15:49

2010 journal article

NMR Solution Structure and DNA-binding Model of the DNA-binding Domain of Competence Protein A


By: C. Hobbs n, B. Bobay n, R. Thompson n, M. Perego* & J. Cavanagh n

author keywords: competence; ComA; NMR; two-component; response regulator
MeSH headings : Amino Acid Sequence; Bacillus subtilis / metabolism; Bacterial Proteins / chemistry; Bacterial Proteins / genetics; Bacterial Proteins / metabolism; DNA / chemistry; DNA / metabolism; DNA-Binding Proteins / chemistry; DNA-Binding Proteins / genetics; DNA-Binding Proteins / metabolism; Escherichia coli Proteins / chemistry; Escherichia coli Proteins / genetics; Escherichia coli Proteins / metabolism; Helix-Turn-Helix Motifs; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Tertiary
TL;DR: Using NMR spectroscopy, the high-resolution 3D solution structure of the C-terminal DNA-binding domain of ComA (ComAC) has been determined and a model of ComAC bound to the ComA recognition sequences on the srfA promoter has been developed, suggesting a basis for DNA binding specificity within the NarL family. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

2009 journal article

Structural Characterization of the Conformational Change in Calbindin-D-28k upon Calcium Binding Using Differential Surface Modification Analyzed by Mass Spectrometry

BIOCHEMISTRY, 48(36), 8603–8614.

By: C. Hobbs n, L. Deterding*, L. Perera*, B. Bobay n, R. Thompson n, T. Darden*, J. Cavanagh n, K. Tomer*

MeSH headings : Amino Acid Sequence; Animals; Apoproteins / chemistry; Calbindin 1; Calbindins; Cysteine / chemistry; Disulfides / chemistry; EF Hand Motifs; Hydrogen Bonding; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Rats; S100 Calcium Binding Protein G / chemistry; S100 Calcium Binding Protein G / metabolism; Spectrometry, Mass, Electrospray Ionization; Tandem Mass Spectrometry
TL;DR: Differential surface modification of lysine and histidine residues analyzed by mass spectrometry has been used in this study to identify, for the first time, the specific regions of calbindin-D28k undergoing conformational changes between the holo and apo states and indicate that there is predominantly no disulfide bond between these residues in the apoprotein. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

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