Works (3)

Updated: July 5th, 2023 15:55

2009 journal article

Structural and Motional Contributions of the Bacillus subtilis ClpC N-Domain to Adaptor Protein Interactions

JOURNAL OF MOLECULAR BIOLOGY, 387(3), 639–652.

By: D. Kojetin*, P. McLaughlin n, R. Thompson n, D. Dubnau, P. Prepiak, M. Rance*, J. Cavanagh n

author keywords: competence; adaptor protein proteosome interactions; HSP100/Clp N-domain; NMR dynamics
MeSH headings : Adaptor Proteins, Vesicular Transport / chemistry; Adaptor Proteins, Vesicular Transport / genetics; Adaptor Proteins, Vesicular Transport / metabolism; Amino Acid Sequence; Bacillus subtilis / genetics; Bacillus subtilis / metabolism; Bacterial Proteins / chemistry; Bacterial Proteins / genetics; Bacterial Proteins / metabolism; Heat-Shock Proteins / chemistry; Heat-Shock Proteins / genetics; Heat-Shock Proteins / metabolism; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Binding; Protein Structure, Secondary; Sequence Alignment; Static Electricity
TL;DR: NMR experiments used to map the MecA adaptor protein interaction surface of N-ClpCR reveal that regions involved in the interaction possess conformational flexibility and conformational exchange on the microsecond-to-millisecond timescale. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

2007 journal article

NMR assignment of the N-terminal repeat domain of Bacillus subtilis ClpC

BIOMOLECULAR NMR ASSIGNMENTS, 1(2), 163–165.

author keywords: ClpC; Bacillus subtilis; N-domain; genetic competence; HSP100/AAA+
MeSH headings : Amino Acid Sequence; Bacterial Proteins / chemistry; Connexins / chemistry; Heat-Shock Proteins / chemistry; Magnetic Resonance Spectroscopy / methods; Protein Structure, Tertiary; Repetitive Sequences, Amino Acid
TL;DR: The backbone and side-chain assignments of the N-terminal repeat domain (residues 1–145) of ClpC from Bacillus subtilis are presented. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

2007 journal article

Predominantly buried residues in the response regulator Spo0F influence specific sensor kinase recognition

FEBS LETTERS, 581(7), 1425–1429.

By: P. McLaughlin n, B. Bobaya, E. Regel n, R. Thompson n, J. Hoch* & J. Cavanagh n

author keywords: sporulation; kinases; Spo0F mutants
MeSH headings : Alanine / chemistry; Alanine / genetics; Amino Acid Sequence; Amino Acid Substitution; Bacillus subtilis / metabolism; Bacillus subtilis / physiology; Bacterial Proteins / chemistry; Bacterial Proteins / genetics; Bacterial Proteins / metabolism; Histidine Kinase; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Protein Interaction Mapping; Protein Kinases / chemistry; Protein Kinases / metabolism; Protein Structure, Secondary; Spores, Bacterial
TL;DR: How buried residues and intra‐protein communication networks contribute to precise molecular recognition by ensuring that the correct surface is presented is discussed. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

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