Folding of circular permutants with decreased contact order: General trend balanced by protein stability

Journal of Molecular Biology

Volumn 314, Issue 4, 2001, Pages 891-900

  Lindberg, Magnus O ^a   Tångrot, Jeanette ^a   Otzen, Daniel E ^b   Dolgikh, Dmitry A ^c   Finkelstein, Alexei V ^d   Oliveberg, Mikael ^a  

^a UMEÅ UNIVERSITY   (Sweden)

^b AALBORG UNIVERSITY   (Denmark)

^c SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

^d INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

Author keywords

Protein folding; Protein stability; Rate constants; Topology; Two state proteins

Indexed keywords

MUTANT PROTEIN; PROTEIN; SODIUM SULFATE;

ARTICLE; CONFORMATIONAL TRANSITION; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; THERMODYNAMICS;

EID: 0035824886     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.5186     Document Type: Article

References (38)

1. Topology, stability, sequence, and length: Defining the determinants of two-state protein folding kinetics
2. Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism
3. The roles of stability and contact order in determining protein folding rates
4. Mechanisms of protein folding
5. Contact order, transition state placement and the refolding rates of single domain proteins
6. Cytochrome b562 folding triggered by electron transfer: Approaching the speed limit for formation of a four-helix-bundle protein
7. Slow folding of muscle acylphosphatase in the absence of intermediates
8. Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates
9. Loop length, intramolecular diffusion and protein folding
10. Single versus parallel pathways of protein folding and fractional formation of structure in the transition state
11. Mapping the transition state and pathway of protein folding by protein engineering
12. The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering: Evidence for a nucleation-condensation mechanism for protein folding
13. Structural changes in the transition state of protein folding: Alternative interpretations of curved chevron plots
14. Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain
15. Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding
16. The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved
17. Experiment and theory highlight role of native state topology in SH3 folding
18. Different circular permutations produced different folding nuclei in proteins: A computational study
19. A simple way to measure protein refolding rates in water
20. Folding of circular and permuted chymotrypsin inhibitor 2: Retention of the folding nucleus
21. The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics
22. Different folding transition states may result in the same native structure
23. Characterisation of the transition states for protein folding: Towards a new level of mechanistic detail in protein engineering analysis
24. Rate of protein folding near the point of thermodynamic equilibrium between the coil and the most stable chain fold
25. Folding nuclei in proteins
26. Theoretical study of a landscape of protein folding-unfolding pathways, folding rates at midtransition
27. Salt-induced detour through compact regions of the protein folding landscape
28. Random circular permutation of DsbA reveals segments that are essential for protein folding and stability
29. Systematic circular permutation of an entire protein reveals essential folding elements
30. Complementation of peptide fragments of the single domain protein chymotrypsin inhibitor 2
31. S6 permutein shows that the unusual target topology is not responsible for the absence of rigid tertiary structure in de novo protein albebetin
32. WHAT IF: A molecular modeling and drug design program
33. Folding of chymotrypsin inhibitor 2.1. Evidence for a two-state transition
34. Protein denaturation
35. Protein denaturation. C. Theoretical models for the mechanism of denaturation
36. How do small single-domain proteins fold?
37. Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9