Chromatinpackung in normalen Spermatozoen und solchen von Männern mit Teratozoospermie Normalgeformte ovale und Teratozoospermie‐Spermatozoen wurden mittels verschiedener Untersuchungstechniken miteinander verglichen ...

The major factor that drives a protein chain toward collapse and folding is the hydrophobic effect. Amino acids with apolar side chains join forming a solvent-shielded hydrophobic core. This process pack the structure in ...

In protein evolution, due to functional and biophysical constraints, the rates of amino acid substitution differ from site to site. Among the best predictors of site-specific rates are solvent accessibility and packing ...

For protein structure to prevail in water, its backbone hydrogen bonds must be shielded from water attack, requiring a cluster of “wrapping” nonpolar groups. Thus, underwrapped regions are adhesive, as exogenous removal ...

We study the time series of the total energy of polypeptides and proteins. These time series were generated by molecular dynamics methods and analyzed by applying detrended fluctuation analysis to estimate the long-range ...

Protein sequences evolve under selection pressures imposed by functional and biophysical requirements, resulting in site-dependent rates of amino acid substitution. Relative solvent accessibility (RSA) and local packing ...

A net dipole moment is shown to arise from a non-Debye component of water polarization created by nanoscale packing defects on the protein surface. Accordingly, the protein electrostatic field exerts a torque on the induced ...

This work explores the possibility of using the electrically charged "spherical soft particle" (SSP) to model the electrophoretic mobility of proteins in the low charge regime. The general framework concerning the ...