Role of topology in the cooperative collapse of the protein core in the sequential collapse model. Folding pathway of (alpha)-lactalbumin and hen lysozyme

Article Abstract:

The cooperative collapse of the protein primary loop in the sequential collapse model (SCM), the application of the SCM model for studying the folding pathways of (alpha)-lactalbumin and the role of topology in the cooperative collapse of the protein core in SCM is explored. The results indicate that the long proteins could form independent primary loops, with each one producing a distinct folding unit.

Topology, Lysozyme, Milk proteins, Algebraic topology

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Sequential collapse folding pathway of beta-lactoglobulin: Parallel pathways and non-native secondary structure

Article Abstract:

The sequential collapse model (SCM) for revealing protein folding pathways is applied to bovine beta-lactoglobulin. An analysis based on the SCM suggests that, in addition to the dominant early intermediate specified by the best predicted primary contact, there are coexisting populations of early intermediates defined by the formation of less energetically favorable primary contacts.

Protein folding, Properties, Globulin, Globulins

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Two-state folding kinetics of small proteins in the sequential collapse model: dependence of the folding rate on contact order and temperature

Article Abstract:

Studies done on the dynamics of the collapse-like folding transitions of globular proteins with two-state kinetics applying sequential collapse model (SCM) is reported. SCM predicts an approximate linear dependence of the folding rate with the contact order and temperature consistent with experimental observations.

Observations, Proteins, Thermal properties, Dynamics, Dynamics (Mechanics)

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