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
JOURNAL OF MOLECULAR BIOLOGY, 398(2), 248–263.
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)
open access via europepmc.org (repository)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
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.
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)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: August 6, 2018
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