The Protein Journal

, Volume 26, Issue 8, pp 556–561

QHELIX: A Computational Tool for the Improved Measurement of Inter-Helical Angles in Proteins


DOI: 10.1007/s10930-007-9097-9

Cite this article as:
Lee, H.S., Choi, J. & Yoon, S. Protein J (2007) 26: 556. doi:10.1007/s10930-007-9097-9


Knowledge about the assembled structures of the secondary elements in proteins is essential to understanding protein folding and functionality. In particular, the analysis of helix geometry is required to study helix packing with the rest of the protein and formation of super secondary structures, such as, coiled coils and helix bundles, formed by packing of two or more helices. Here we present an improved computational method, QHELIX, for the calculation of the orientation angles between helices. Since a large number of helices are known to be in curved shapes, an appropriate definition of helical axes is a prerequisite for calculating the orientation angle between helices. The present method provides a quantitative measure on the irregularity of helical shape, resulting in discriminating irregular-shaped helices from helices with an ideal geometry in a large-scale analysis of helix geometry. It is also capable of straightforwardly assigning the direction of orientation angles in a consistent way. These improvements will find applications in finding a new insight on the assembly of protein secondary structure.


Helical axisInter-helical angleProtein structureQHELIX, computational tool



Protein data bank


Nuclear magnetic resonance


Staphylococcal protein A

Supplementary material

10930_2007_9097_MOESM1_ESM.pdf (21 kb)
ESM1 (PDF 21 KB)

Copyright information

© Springer Science+Business Media, LLC 2007

Authors and Affiliations

  1. 1.Department of Biological Sciences, Research Center for Women’s Diseases (RCWD)Sookmyung Women’s UniversitySeoulRepublic of Korea