Supported by Research Grants from the National Institutes of Health, U.S. Public Health Service (GM-12157) and the National Science Foundation (GB-16420).
Research Career Development Awardee of the National Institutes of Health, U.S. Public Health Service (Grant GM-22015).
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Abbreviations
- K:
-
Equilibrium constant for folding
- K':
-
Equilibrium constant for unfolding
- K unf :
-
Same as K'
- k 0i :
-
Rate constant for folding a site with i folded neighbors
- k 1i :
-
Rate constant for unfolding a site with i folded neighbors
- ki :
-
Rate constant for forming species i + 1 from species i
- Ki :
-
Equilibrium constant for forming species i from species 0
- ks :
-
Steady state rate constant
- k ox :
-
Exchange rate constant for free peptide hydrogens
- li :
-
Rate constant for forming species i from species i + 1
- M:
-
Number of contacts in a completely folded lattice
- N:
-
Total number of sites in the lattice
- p:
-
Equilibrium constant for folding a site
- P:
-
Number of ways of realizing a given conformation
- q:
-
Equilibrium constant for forming a contact between two folded sites
- s:
-
Equilibrium constant for helix growth
- t:
-
temperature in °C; time
- T:
-
Temperature in °K
- w:
-
Equilibrium constant for forming a specified conformation
- z:
-
Partition function
- θ:
-
Degree of folding
- θ′:
-
Degree of unfolding
- θ′i :
-
Degree of unfolding for site (type) i
- μ:
-
Number of contacts between folded sites
- ν:
-
Number of sites which are folded
- σ:
-
Equilibrium constant for helix initiation
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Hermans, J., Lohr, D., Ferro, D. (1972). Treatment of the folding and unfolding of protein molecules in solution according to a lattice model. In: Fortschritte der Hochpolymeren-Forschung. Advances in Polymer Science, vol 9. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-05484-7_18
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