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Solution structure and dynamics of the mitochondrial‐targeted GTPase ‐activating protein (GAP) VopE by an integrated NMR / SAXS approach

https://doi.org/10.1002/pro.4282

Smith, Kyle P.; Lee, Woonghee; Tonelli, Marco; Lee, Yeongjoon; Light, Samuel H.; Cornilescu, Gabriel; Chakravarthy, Srinivas (May 2022, Protein Science)

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Conformational Switch to a β-Turn in a Staphylococcal Quorum Sensing Signal Peptide Causes a Dramatic Increase in Potency

https://doi.org/10.1021/jacs.9b05513

Vasquez, Joseph K.; West, Korbin H.; Yang, Tian; Polaske, Thomas J.; Cornilescu, Gabriel; Tonelli, Marco; Blackwell, Helen E. (December 2019, Journal of the American Chemical Society)

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Structural Characterization of Competence-Stimulating Peptide Analogues Reveals Key Features for ComD1 and ComD2 Receptor Binding in Streptococcus pneumoniae

https://doi.org/10.1021/acs.biochem.8b00653

Yang, Yifang; Cornilescu, Gabriel; Tal-Gan, Yftah (August 2018, Biochemistry)

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Function and solution structure of the Arabidopsis thaliana RALF8 peptide

https://doi.org/10.1002/pro.3628

Frederick, Ronnie O.; Haruta, Miyoshi; Tonelli, Marco; Lee, Woonghee; Cornilescu, Gabriel; Cornilescu, Claudia C.; Sussman, Michael R.; Markley, John L. (May 2019, Protein Science)

Abstract We report the recombinant preparation fromEscherichia colicells of samples of two closely related, small, secreted cysteine‐rich plant peptides: rapid alkalinization factor 1 (RALF1) and rapid alkalinization factor 8 (RALF8). Purified samples of the native sequence of RALF8 exhibited well‐resolved nuclear magnetic resonance (NMR) spectra and also biological activity through interaction with a plant receptor kinase, cytoplasmic calcium mobilization, andin vivoroot growth suppression. By contrast, RALF1 could only be isolated from inclusion bodies as a construct containing an N‐terminal His‐tag; its poorly resolved NMR spectrum was indicative of aggregation. We prepared samples of the RALF8 peptide labeled with¹⁵N and¹³C for NMR analysis and obtained near complete¹H,¹³C, and¹⁵N NMR assignments; determined the disulfide pairing of its four cysteine residues; and examined its solution structure. RALF8 is mostly disordered except for the two loops spanned by each of its two disulfide bridges.
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