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The lower parts of the walls of the 16th century dining hall of St John's College, Cambridge are covered with wood panelling in a linenfold design. An English oak chest with complex linenfold panels.
Coarse-grained modeling, coarse-grained models, aim at simulating the behaviour of complex systems using their coarse-grained (simplified) representation. Coarse-grained models are widely used for molecular modeling of biomolecules [1] [2] at various granularity levels.
Levinthal's paradox is a thought experiment in the field of computational protein structure prediction; protein folding seeks a stable energy configuration. An algorithmic search through all possible conformations to identify the minimum energy configuration (the native state) would take an immense duration; however in reality protein folding happens very quickly, even in the case of the most ...
The word linen is of West Germanic origin [4] and cognate to the Latin name for the flax plant, linum, and the earlier Greek λινόν (linón).. This word history has given rise to a number of other terms in English, most notably line, from the use of a linen (flax) thread to determine a straight line.
The hydrophobic-polar protein folding model is a highly simplified model for examining protein folds in space. First proposed by Ken Dill in 1985, it is the most known type of lattice protein: it stems from the observation that hydrophobic interactions between amino acid residues are the driving force for proteins folding into their native state. [1]
In science, e-folding is the time interval in which an exponentially growing quantity increases or decreases by a factor of e; [1] it is the base-e analog of doubling time. This term is often used in many areas of science, such as in atmospheric chemistry , medicine , theoretical physics , and cosmology .
In molecular biology, protein threading, also known as fold recognition, is a method of protein modeling which is used to model those proteins which have the same fold as proteins of known structures, but do not have homologous proteins with known structure.
The Rossmann fold is a tertiary fold found in proteins that bind nucleotides, such as enzyme cofactors FAD, NAD +, and NADP +.This fold is composed of alternating beta strands and alpha helical segments where the beta strands are hydrogen bonded to each other forming an extended beta sheet and the alpha helices surround both faces of the sheet to produce a three-layered sandwich.