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Treatment of the folding and unfolding of protein molecules in solution according to a lattice model

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Fortschritte der Hochpolymeren-Forschung

Part of the book series: Advances in Polymer Science ((POLYMER,volume 9))

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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