Patrick Daniel McLaughlin

Works (3)

Updated: July 5th, 2023 15:55

2009 article

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

Kojetin, D. J., McLaughlin, P. D., Thompson, R. J., Dubnau, D., Prepiak, P., Rance, M., & Cavanagh, J. (2009, January 31). Journal of Molecular Biology.

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
topics (OpenAlex): Protein Structure and Dynamics; Bacterial Genetics and Biotechnology; Enzyme Structure and Function
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)
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Source: Web Of Science
Added: August 6, 2018

2007 article

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

Kojetin, D. J., McLaughlin, P. D., Thompson, R. J., Venters, R. A., Rance, M., & Cavanagh, J. (2007, September 5). Biomolecular NMR Assignments.

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

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
topics (OpenAlex): Bacterial Genetics and Biotechnology; Protein Structure and Dynamics; RNA and protein synthesis mechanisms
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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Added: August 6, 2018

2007 article

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

McLaughlin, P. D., Bobay, B. G., Regel, E. J., Thompson, R. J., Hoch, J. A., & Cavanagh, J. (2007, March 5). FEBS Letters.

By: P. McLaughlin n, B. Bobay n, 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
topics (OpenAlex): Bacterial Genetics and Biotechnology; Protein Structure and Dynamics; Enzyme Structure and Function
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)
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Source: Web Of Science
Added: August 6, 2018

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