Alex Hansen

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We present a statistical mechanics treatment of the stability of globular proteins which takes explicitly into account the coupling between the protein and water degrees of freedom. This allows us to describe both the cold and the warm unfolding, thus qualitatively reproducing the known thermodynamics of proteins. The folded conformation of globular(More)
Thermodynamic measurements of proteins indicate that the folding to the native state takes place either through stable intermediates or through a two-state process without intermediates. The rather short folding times of proteins indicate that folding is guided through some sequence of contact bindings. We discuss the possibility of reconciling a two-state(More)
We refine a protein model that reproduces fundamental aspects of protein thermodynamics. The model exhibits two transitions, hot and cold unfolding. The number of relevant parameters is reduced to three: (1) binding energy of folding relative to the orientational energy of bound water, (2) ratio of degrees of freedom between the folded and unfolded protein(More)
We review a statistical mechanics treatment of the stability of globular proteins based on a simple model Hamiltonian taking into account protein self interactions and protein-water interactions. The model contains both hot and cold folding transitions. In addition it predicts a critical point at a given temperature and chemical potential of the surrounding(More)
The statistics of damage avalanches during a failure process typically follows a power law. When these avalanches are recorded only near the point at which the system fails catastrophically, one finds that the power law has an exponent which is different from that one finds if the recording of events starts away from the vicinity of catastrophic failure. We(More)
We propose a protein model based on a hierarchy of constraints that force the protein to follow certain pathways when changing conformation. The model exhibits a first order phase transition, cooperativity and is exactly solvable. It also shows an unexpected symmetry between folding and unfolding pathways as suggested by a recent experiment. Proteins(More)
The roughness of crack interfaces is reported in quasistatic fracture, using an elastic network of beams with random breaking thresholds. For strong disorders we obtain zeta = 0.86(3) for the roughness exponent, a result which is very different from the minimum energy surface exponent, i.e., zeta = 2 / 3. A crossover to lower values is observed as the(More)
The presence of lower cutoff in fiber threshold distribution may affect the failure properties of a bundle of fibers subjected to external load. We investigate this possibility--both in an equal load sharing (ELS) model and in a local load sharing (LLS) one using analytic as well as numerical methods. In the ELS model, the critical strength gets modified(More)