Figure - PMC

Skip to main content

View full-text article in PMC

. Author manuscript; available in PMC: 2009 Sep 6.

Published in final edited form as: J Mol Biol. 2007 Dec 4;376(3):736–748. doi: 10.1016/j.jmb.2007.11.075

(a) ¹H-¹⁵N HSQC spectrum of peptide GF at 10°C. Sequence diagram of the peptide above the HSQC shows the characteristic one residue stagger. The isotope-labeled residues are colored in blue. All labeled residues Gly13, Phe14 and Gly24 have trimer peaks as well as monomer peaks, showing the GF interruption is incorporated into a trimer. The peaks corresponding to the monomer and trimer state are denoted with a superscript M or T, respectively. Leading, middle, or trailing chain stagger assignment is indicated as chain 1, 2, or 3 by a number in front of the superscript T.

(b) Contact map generated from NH-H experimental NOEs from the NOESY-HSQC experiment for the GF peptide. Experimental NOEs for GF peptide are represented by circles (HN-HN(), HN-H^α(), and HN-side chain protons()). Intrachain NOEs are shaded in gray. Interchain contacts are consistent with one residue staggering of triple helix.

(c) Experimental ³J_HNHa coupling constants of peptide GF. ³J_HNHa coupling constants for Gly13, Phe14 and Gly24, with the two H^α Gly residues shown as dark gray and light gray bars.

Inline graphic — (a) ¹H-¹⁵N HSQC spectrum of peptide GF at 10°C. Sequence diagram of the peptide above the HSQC shows the characteristic one residue stagger. The isotope-labeled residues are colored in blue. All labeled residues Gly13, Phe14 and Gly24 have trimer peaks as well as monomer peaks, showing the GF interruption is incorporated into a trimer. The peaks corresponding to the monomer and trimer state are denoted with a superscript M or T, respectively. Leading, middle, or trailing chain stagger assignment is indicated as chain 1, 2, or 3 by a number in front of the superscript T.

(b) Contact map generated from NH-H experimental NOEs from the NOESY-HSQC experiment for the GF peptide. Experimental NOEs for GF peptide are represented by circles (HN-HN(), HN-H^α(), and HN-side chain protons()). Intrachain NOEs are shaded in gray. Interchain contacts are consistent with one residue staggering of triple helix.

(c) Experimental ³J_HNHa coupling constants of peptide GF. ³J_HNHa coupling constants for Gly13, Phe14 and Gly24, with the two H^α Gly residues shown as dark gray and light gray bars.