Hostname: page-component-586b7cd67f-2plfb Total loading time: 0 Render date: 2024-11-24T07:20:15.737Z Has data issue: false hasContentIssue false

A molecular dynamics study of the 41–56 β-hairpin from B1 domain of protein G

Published online by Cambridge University Press:  01 October 1999

DANILO ROCCATANO
Affiliation:
Groningen Biomolecular Sciences and Biotechnology Institute (GBB), Department of Biophysical Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
ANDREA AMADEI
Affiliation:
Dipartimento di Chimica, Università di Roma (La Sapienza), P. le A. Moro 5, 00185 Rome, Italy
ALFREDO DI NOLA
Affiliation:
Dipartimento di Chimica, Università di Roma (La Sapienza), P. le A. Moro 5, 00185 Rome, Italy
HERMAN J.C. BERENDSEN
Affiliation:
Groningen Biomolecular Sciences and Biotechnology Institute (GBB), Department of Biophysical Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Get access

Abstract

The structural and dynamical behavior of the 41–56 β-hairpin from the protein G B1 domain (GB1) has been studied at different temperatures using molecular dynamics (MD) simulations in an aqueous environment. The purpose of these simulations is to establish the stability of this hairpin in view of its possible role as a nucleation site for protein folding. The conformation of the peptide in the crystallographic structure of the protein GB1 (native conformation) was lost in all simulations. The new equilibrium conformations are stable for several nanoseconds at 300 K (>10 ns), 350 K (>6.5 ns), and even at 450 K (up to 2.5 ns). The new structures have very similar hairpin-like conformations with properties in agreement with available experimental nuclear Overhauser effect (NOE) data. The stability of the structure in the hydrophobic core region during the simulations is consistent with the experimental data and provides further evidence for the role played by hydrophobic interactions in hairpin structures. Essential dynamics analysis shows that the dynamics of the peptide at different temperatures spans basically the same essential subspace. The main equilibrium motions in this subspace involve large fluctuations of the residues in the turn and ends regions. Of the six interchain hydrogen bonds, the inner four remain stable during the simulations. The space spanned by the first two eigenvectors, as sampled at 450 K, includes almost all of the 47 different hairpin structures found in the database. Finally, analysis of the hydration of the 300 K average conformations shows that the hydration sites observed in the native conformation are still well hydrated in the equilibrium MD ensemble.

Type
Research Article
Copyright
© 1999 The Protein Society

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)