Structural analysis of protein dynamics by MD simulations and NMR spin-relaxation
نویسندگان
چکیده
منابع مشابه
Protein dynamics at Eph receptor-ligand interfaces as revealed by crystallography, NMR and MD simulations
BACKGROUND The role of dynamics in protein functions including signal transduction is just starting to be deciphered. Eph receptors with 16 members divided into A- and B- subclasses are respectively activated by 9 A- and B-ephrin ligands. EphA4 is the only receptor capable of binding to all 9 ephrins and small molecules with overlapped interfaces. RESULTS We first determined the structures of...
متن کاملProtein Dynamics by NMR Spin Relaxation: The Slowly Relaxing Local Structure Perspective
Protein dynamics by NMR has been reviewed extensively in recent years.1 – 4 These surveys show convincingly that information on structure has to be complemented by information on motion to properly characterize proteins and understand their function. The timescale accessible by NMR extends from picoseconds to days. Heteronuclear NMR spin relaxation applies to the picoseconds to nanoseconds regi...
متن کاملThe dynamics of lysozyme from bacteriophage lambda in solution probed by NMR and MD simulations.
(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 ...
متن کاملDynamics and Chemical Shielding in a Small Protein from NMR Spin Relaxation Experiments
Title of Dissertation: Dynamics and Chemical Shielding in a Small Protein from NMR Spin Relaxation Experiments Jennifer Blake Hall, Doctor of Philosophy, 2006 Directed By: Prof. David Fushman Department of Chemistry and Biochemistry NMR spin relaxation spectroscopy is a proven method for characterization of the timescales and amplitudes of intramolecular motions in proteins. In a typical NMR re...
متن کاملThe structural analysis of protein-protein interactions by NMR spectroscopy.
A comprehensive understanding of protein-protein interactions is an important next step in our quest to understand how the information contained in a genome is put into action. Although a number of experimental techniques can report on the existence of a protein- protein interaction, very few can provide detailed structural information. NMR spectroscopy is one of these, and in recent years seve...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Proteins: Structure, Function, and Bioinformatics
سال: 2008
ISSN: 0887-3585,1097-0134
DOI: 10.1002/prot.21750