Related Experiment Video
Updated: Aug 2, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Solution conformations of human growth hormone releasing factor: comparison of the restrained molecular dynamics and
A T Brünger1, G M Clore, A M Gronenborn
1Department of Chemistry, Harvard University, Cambridge, MA 02138.
Abstract:
A series of three-dimensional structures of the 1-29 fragment of human growth hormone releasing factor in trifluoroethanol have been determined by molecular dynamics and distance geometry methods. The resulting structures satisfy information from nuclear Overhauser effect (NOE) distance data and an empirical potential energy function. Although the polypeptide was found to have an ordered structure in all simulations, the NOE data were not sufficient for global convergence to a unique three-dimensional geometry. Several satisfactory structures have been determined, all of which are extended conformations consisting of a short beta-strand and two alpha-helices (residues 6-13 and residues 16-29) connected by short segments of less well defined secondary structure. Because of the lack of NOE data connecting the helix segments, their relative orientation is not uniquely determined.
Related Concept Videos
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Newman Projections
The organic molecules rotate across the single bonds leading to numerous temporary three-dimensional structures of varying energy known as conformers.
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

