help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH

Biophys. J. BioFAST: First Published July 29, 2005. doi:10.1529/biophysj.105.065904
© 2005 by the Biophysical Society.


A more recent version of this article appeared on October 1, 2005.
This Article
Right arrow Full Text (Rapid PDF)
Right arrow All Versions of this Article:
biophysj.105.065904v1
89/4/2395    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by lu, m.
Right arrow Articles by Ma, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by lu, m.
Right arrow Articles by Ma, J.

BIOPHYSICAL THEORY AND MODELING

The Role of Shape in Determining Molecular Motions

mingyang lu 1 and Jianpeng Ma 1*

1 Baylor College of Medicine

* To whom correspondence should be addressed. E-mail: jpma{at}bcm.tmc.edu.

Submitted on May 5, 2005
Revised on June 9, 2005
Accepted on 15 July 2005


   Abstract
We examined the role of molecular shape in determining the patterns of low-frequency deformational motions of biological macromolecules. The low-frequency subspace of eigenvectors in normal mode analysis was found to be robustly similar upon randomization of the Hessian matrix elements as long as the structure of the matrix is maintained, which indicates that the global shape of molecule plays a more dominant role in determining the highly anisotropic low-frequency motions than the absolute values of stiffness and directionality of local interactions. The results provided a quantitative foundation for the validity of elastic normal mode analysis.

Key Words: Conformational motion, anisotropy, normal mode analysis, shape




This article has been cited by other articles:


Home page
Biophys. JHome page
M. M. Gibbons and W. S. Klug
Influence of Nonuniform Geometry on Nanoindentation of Viral Capsids
Biophys. J., October 15, 2008; 95(8): 3640 - 3649.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
M. Lu and J. Ma
A minimalist network model for coarse-grained normal mode analysis and its application to biomolecular x-ray crystallography
PNAS, October 7, 2008; 105(40): 15358 - 15363.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
B. Isin, K. Schulten, E. Tajkhorshid, and I. Bahar
Mechanism of Signal Propagation upon Retinal Isomerization: Insights from Molecular Dynamics Simulations of Rhodopsin Restrained by Normal Modes
Biophys. J., July 15, 2008; 95(2): 789 - 803.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
G. Cui and K. M. Merz Jr.
The Intrinsic Dynamics and Function of Nickel-Binding Regulatory Protein: Insights from Elastic Network Analysis
Biophys. J., May 15, 2008; 94(10): 3769 - 3778.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
T. Z. Sen, M. Kloster, R. L. Jernigan, A. Kolinski, J. M. Bujnicki, and A. Kloczkowski
Predicting the Complex Structure and Functional Motions of the Outer Membrane Transporter and Signal Transducer FecA
Biophys. J., April 1, 2008; 94(7): 2482 - 2491.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
J. G. Su, X. Jiao, T. G. Sun, C. H. Li, W. Z. Chen, and C. X. Wang
Analysis of Domain Movements in Glutamine-Binding Protein with Simple Models
Biophys. J., February 15, 2007; 92(4): 1326 - 1335.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Copyright © 2005 by the Biophysical Society.