2005/09/15 by Samuel Nicolay, Yves‐Henri Sanejouand, Yves-Henri Sanejouand · 4 citations
Biochemistry, Genetics and Molecular Biology · Materials Science · Physics and Astronomy · #Enzyme Structure and Function #Protein Structure and Dynamics #Spectroscopy and Quantum Chemical Studies #q-bio.BM
paper · pdf · doi:10.1103/physrevlett.96.078104
published as Phys. Rev. Letters vol. 96 078104 (2006) · 4 pages, 5 figures
arxiv created 2005/09/15 · openalex publication_date 2006/02/24 · arxiv updated 2009/12/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28
It is shown that a small subset of modes which are likely to be involved in protein functional motions of large amplitude can be determined by retaining the most robust normal modes obtained using different protein models. This result should prove helpful in the context of several applications proposed recently, like for solving difficult molecular replacement problems or for fitting atomic structures into low-resolution electron density maps. It may also pave the way for the development of methods allowing us to predict such motions accurately.