Site-selective intramolecular hydrogen-bonding interactions in phosphorylated serine and threonine dipeptides

Kyung Koo Lee, Eunmyung Kim, Cheonik Joo, Jaewook Song, Hogyu Han, Minhaeng Cho

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)


To study the phosphorylation effect on the peptide conformation, we carried out nuclear magnetic resonance (NMR), circular dichroism (CD), Fourier transform (FT)-IR, and vibrational circular dichroism (VCD) experiments with serine and threonine dipeptides (SD and TD) and their phosphorylated ones (pSD and pTD). It is found that both unphosphorylated and phosphorylated serine and threonine dipeptides adopt two conformations, polyproline II (PII) and β-strand. The pH-dependent NMR study shows that the side-chain dianionic phosphoryl group can form direct intramolecular hydrogen bonds with the backbone amide protons at both the acetyl and amide ends of pTD, but only at the acetyl end of pSD. Temperature- and pH-dependent CD studies reveal that, unlike pSD, pTD undergoes conformational transition from PII to β-strand upon double ionization of the phosphoryl group. The subtle but distinct differences between pTD and pSD in site-selective intramolecular hydrogen-bonding interaction and charge-dependent conformational transition may sometimes become significant when choosing between serine and threonine for the conformational control of peptides and proteins by phosphorylation.

Original languageEnglish
Pages (from-to)16782-16787
Number of pages6
JournalJournal of Physical Chemistry B
Issue number51
Publication statusPublished - 2008 Dec 25

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry


Dive into the research topics of 'Site-selective intramolecular hydrogen-bonding interactions in phosphorylated serine and threonine dipeptides'. Together they form a unique fingerprint.

Cite this