Analysis of protein dynamics using local-DME calculations

Thumbnail Image
Date
2011-01-01
Authors
Wu, Di
Smith, Stephen
Mahan, Hannah
Jernigan, Robert
Wu, Zhijun
Major Professor
Advisor
Committee Member
Journal Title
Journal ISSN
Volume Title
Publisher
Authors
Person
Jernigan, Robert
Distinguished Professor
Research Projects
Organizational Units
Organizational Unit
Organizational Unit
Mathematics
Welcome to the exciting world of mathematics at Iowa State University. From cracking codes to modeling the spread of diseases, our program offers something for everyone. With a wide range of courses and research opportunities, you will have the chance to delve deep into the world of mathematics and discover your own unique talents and interests. Whether you dream of working for a top tech company, teaching at a prestigious university, or pursuing cutting-edge research, join us and discover the limitless potential of mathematics at Iowa State University!
Journal Issue
Is Version Of
Versions
Series
Department
Biochemistry, Biophysics and Molecular BiologyMathematics
Abstract

Flexibility and dynamics of protein structures are reflected in the B-factors and order parameters obtained experimentally with X-ray crystallography and Nuclear Magnetic Resonance (NMR). Methods such as Normal Mode Analysis (NMA) and Elastic Network Models (ENM) can be used to predict the fluctuations of protein structures for either atomic level or coarse-grained structures. Here, we introduce the Local-Distance Matrix Error (DME), an efficient and simple analytic method to study the fluctuations of protein structures, especially for the ensembles of NMR-determined protein structures. Comparisons with the fluctuations obtained by experiments and other by computations show strong correlations.

Comments

This is a manuscript of an article published as Wu, Di, Stephen Smith, Hannah Mahan, Robert L. Jernigan, and Zhijun Wu. "Analysis of protein dynamics using local-DME calculations." International journal of bioinformatics research and applications 7, no. 2 (2011): 146-161. doi: 10.1504/IJBRA.2011.040093. Posted with permission.

Description
Keywords
Citation
DOI
Copyright
Sat Jan 01 00:00:00 UTC 2011
Collections