K
Kelvin B. Rembert
Researcher at Pennsylvania State University
Publications - 12
Citations - 1195
Kelvin B. Rembert is an academic researcher from Pennsylvania State University. The author has contributed to research in topics: Hofmeister series & Chemistry. The author has an hindex of 8, co-authored 10 publications receiving 940 citations. Previous affiliations of Kelvin B. Rembert include University of Utah & Texas A&M University.
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Journal ArticleDOI
Beyond the Hofmeister Series: Ion-Specific Effects on Proteins and Their Biological Functions
Halil I. Okur,Jana Hladílková,Kelvin B. Rembert,Younhee Cho,Jan Heyda,Joachim Dzubiella,Joachim Dzubiella,Paul S. Cremer,Pavel Jungwirth +8 more
TL;DR: It is shown that the cationic and anionic Hofmeister series can now be rationalized primarily in terms of specific interactions of salt ions with the backbone and charged side chain groups at the protein surface in solution.
Journal ArticleDOI
Molecular mechanisms of ion-specific effects on proteins.
TL;DR: The specific binding sites of Hofmeister ions with an uncharged 600-residue elastin-like polypeptide, (VPGVG)(120), were elucidated using a combination of NMR and thermodynamic measurements along with molecular dynamics simulations and provide new insights into the mechanism of peptide-anion interactions.
Journal ArticleDOI
Reversal of the Hofmeister Series: Specific Ion Effects on Peptides
Jana Paterová,Kelvin B. Rembert,Jan Heyda,Yadagiri Kurra,Halil I. Okur,Wenshe R. Liu,Christian Hilty,Paul S. Cremer,Pavel Jungwirth +8 more
TL;DR: In this paper, it was shown that the Hofmeister ordering of anions changes from a direct to a reversed series upon uncapping the N-terminus of the peptide bond.
Journal Article
Reversal of the Hofmeister Series: Specific Ion Effects on Peptides B
Jana Paterová,Kelvin B. Rembert,Jan Heyda,Yadagiri Kurra,HalilI. Okur,Wenshe R. Liu,Christian Hilty,Paul S. Cremer,Pavel Jungwirth +8 more
TL;DR: The present study provides a molecular rationalization of Hofmeister ordering for the anions and provides a route for tuning these interactions by titration or mutation of basic amino acid residues on the protein surface by means of NMR spectroscopy and molecular dynamics simulations.
Journal ArticleDOI
Guanidinium can both Cause and Prevent the Hydrophobic Collapse of Biomacromolecules
Jan Heyda,Halil I. Okur,Jana Hladílková,Kelvin B. Rembert,William Hunn,Tinglu Yang,Joachim Dzubiella,Joachim Dzubiella,Pavel Jungwirth,Paul S. Cremer +9 more
TL;DR: A detailed, molecular-level, mechanistic picture is provided of how Gnd+ influences the stability of polypeptides in three distinct physical regimes by varying the anion, which helps explain the circumstances under which guanidinium salts can act as powerful and versatile protein denaturants.