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Updated: Jun 22, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
On the occurrence of linear groups in proteins
Scott A Hollingsworth1, Donald S Berkholz, P Andrew Karplus
1Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331-7305, USA.
Protein structures reveal only three main polypeptide conformations exist: extended beta-strands, polyproline-II-like spirals, and alpha-helices. This empirical study corrects long-held textbook misconceptions about protein structures.
Area of Science:
- Protein structure analysis
- Structural bioinformatics
- Biophysics
Background:
- Linear groups, defined by repeating phi,psi-angles, are fundamental to protein structure.
- Current textbook representations are based on outdated theoretical models.
Purpose of the Study:
- To empirically assess and systematically categorize existing linear groups in proteins.
- To correct misconceptions in protein structure education.
Main Methods:
- Conformation-based survey of ultra-high resolution protein structures.
- Analysis of repeating phi,psi-angle pairs.
Main Results:
- Identified three dominant phi,psi-regions: extended conformations (beta-strands), polyproline-II-like spirals, and a cluster including alpha- and 3(10)-helices.
- Debunked the existence of 2.2(7)- and pi-helices as common linear groups.
- Found no significant phi,psi-preference differences between parallel and antiparallel beta-strands.
Conclusions:
- Protein structure is simpler than often taught, with only three prevalent linear groups.
- This empirical data provides a basis for updating protein structure teaching.
- Clarified the conformational landscape of polypeptide backbones.
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