Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

(15) N NMR relaxation studies, analyses of NMR data to include chemical shifts, residual dipolar couplings (RDC), NOEs and H(N) -H(α) coupling constants, and molecular dynamics (MD) simulations have been used to characterise the behaviour of lysozyme from bacteriophage lambda (λ lysozyme) in solution. The lower and upper lip regions in λ lysozyme (residues 51-60 and 128-141, respectively) show reduced (1) H-(15) N order parameters indicating mobility on a picosecond timescale. In addition, residues in the lower and upper lips also show exchange contributions to T2 indicative of slower timescale motions. The chemical shift, RDC, coupling constant and NOE data for λ lysozyme indicate that two fluctuating β-strands (β3 and β4) are populated in the lower lip region while the N terminus of helix α6 (residues 136-139) forms dynamic helical turns in the upper lip region. This behaviour is confirmed by MD simulations that show hydrogen bonds, indicative of the β-sheet and helical secondary structure in the lip regions, with populations of 40-60 %. Thus in solution λ lysozyme adopts a conformational ensemble that will contain both the open and closed forms observed in the crystal structures of the protein.

Original publication

DOI

10.1002/cbic.201300193

Type

Journal article

Journal

Chembiochem

Publication Date

23/09/2013

Volume

14

Pages

1780 - 1788

Keywords

15N relaxation, NMR spectroscopy, lysozymes, molecular dynamics, residual dipolar couplings, Bacteriophage lambda, Crystallography, X-Ray, Hydrogen Bonding, Molecular Dynamics Simulation, Muramidase, Nitrogen Isotopes, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Secondary, Solutions, Substrate Specificity