Amino Acid Propensities are Position-dependent Throughout the Length of α-Helices
- 9 April 2004
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 337 (5) , 1195-1205
- https://doi.org/10.1016/j.jmb.2004.02.004
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Effect of the N2 residue on the stability of the α‐helix for all 20 amino acidsProtein Science, 2001
- Effect of the N1 residue on the stability of the α‐helix for all 20 amino acidsProtein Science, 2001
- Helix design, prediction and stabilityCurrent Opinion in Biotechnology, 1995
- N‐ and C‐capping preferences for all 20 amino acids in α‐helical peptidesProtein Science, 1995
- Structure Prediction: How good are we?Current Biology, 1995
- Predicting the conformation of proteins from sequences. Progress and future progressJournal of Molecular Recognition, 1995
- Protein Structure Prediction: Recognition of Primary, Secondary, and Tertiary Structural Features from Amino Acid SequenceCritical Reviews in Biochemistry and Molecular Biology, 1995
- Structure prediction of proteins—where are we now?Current Opinion in Biotechnology, 1994
- Design of helix endsInternational Journal of Peptide and Protein Research, 1993
- Helix Signals in ProteinsScience, 1988