Importance of long-range interactions in protein folding
- 10 March 1999
- journal article
- Published by Elsevier in Biophysical Chemistry
- Vol. 77 (1) , 49-68
- https://doi.org/10.1016/s0301-4622(99)00010-1
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Influence of proline residues on protein conformationPublished by Elsevier ,2004
- Recognition of analogous and homologous protein folds--assessment of prediction success and associated alignment accuracy using empirical substitution matricesProtein Engineering, Design and Selection, 1998
- Short-range conformational energies, secondary structure propensities, and recognition of correct sequence-structure matchesProteins-Structure Function and Bioinformatics, 1997
- Consistency in structural energetics of protein folding and peptide recognitionProtein Science, 1997
- A statistical analysis of side-chain conformations in proteins: Comparison with ECEPP predictionsProtein Journal, 1994
- Correlated mutations and residue contacts in proteinsProteins-Structure Function and Bioinformatics, 1994
- On the Conformational Stability of Folded ProteinsJournal of Theoretical Biology, 1994
- The role of local tight packing of hydrophobic groups in β‐structureProteins-Structure Function and Bioinformatics, 1993
- Nonlocal interactions stabilize compact folding intermediates in reduced unfolded bovine pancreatic trypsin inhibitorBiochemistry, 1992
- Analysis of non-polar regions in proteinsJournal of Molecular Biology, 1992