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Normal modes for specific motions of macromolecules: application to the hinge-bending mode of lysozyme.

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Brooks, B, Karplus, M·1985·Proceedings of the National Academy of Sciences

Abstract

A method is presented for finding particular normal modes for large molecules such as proteins and nucleic acids. The method is based on an iterative approach that extracts eigenvectors of interest from the full second-derivative matrix. Application of the method to the interdomain (hinge-bending) motion of lysozyme yields a frequency of 3.6 cm-1. This is similar to the value obtained from earlier adiabatic-energy-minimization studies. Analysis of the mode shows that the relaxation associated with the hinge bending is highly delocalized; that is, the dihedral angle and energy changes are distributed over many residues, including some (e.g., Trp-28) that are distant from the cleft and hinge region.

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Metadata

Authors
Brooks, B., & Karplus, M.
Venue
Proceedings of the National Academy of Sciences
Published
1985-08
Volume
82
Issue
15
Pages
4995-4999
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2068128475
Cited by
342
References
0
FWCI
0.88
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Normal modes for specific motions of macromolecules: application to the hinge-bending mode of lysozyme. https://app.cochat.ai/papers/10.1073/pnas.82.15.4995
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Brooks, B., & Karplus, M. (1985). Normal modes for specific motions of macromolecules: application to the hinge-bending mode of lysozyme. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.82.15.4995

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.