The current geometric and thermodynamic approaches in protein folding studies do not provide a definite solution to understanding mechanisms of folding of biological proteins. A major problem is that the protein is first synthesized as a linear molecule that subsequently must reach its native configuration in an extremely short time. Hydrophobicity-hydrophilicity models and random search mechanism cannot explain folding to the 3-D functional form in less than 1 second, as it occurs in the intact cell. We propose an integral approach, based on the embedding of proteins in the whole cellular context under the postulate: a life protein is never alone. In this concept the protein molecule is influenced by various long and short distance force fields of nature such as coherent electromagnetic waves and zero-point energy. In particular, the role of solitons is reviewed in relation to a novel GM-scale biophysical principle, revealed by us. This recent finding of a set of discrete EM frequency bands, that either promote or endanger life conditions, could be a key in further studies directed at the morphogenetic aspects of protein folding in a biological evolutionary context. In addition, an alternative hypothesis is presented in which each individual cell may store integral 3-D information holographically at the virtual border of a 4-D hypersphere that surrounds each living cell, providing a field receptive memory structure that is instrumental in guiding the folding process towards coherently oscillating protein networks that are crucial for cell survival.(hydrophobic-hydrophilic) model, is extremely complex (i.e., generally requires an enormous number of steps [2]. Levinthal concluded rightfully that a random search can only be performed in an unrealistic timeframe of billions of years [1]. Thus two major questions remain: what are the actual folding mechanisms and how can this ultra-rapid process be realized in the whole, intact, cell structure?Martinez noted that the current folding models had weak predictive ability [3]. Natural proteins consist of 100 to 500 building blocks (alpha-amino-acids), but a random search mechanism cannot provide real-time folding on the order of 1 sec. for these proteins. In the framework of a funnel-like energy landscape, the author considers a simple kinetic model of protein folding. However, this kinetic model assumes that once a domain reaches the correct state, it stays there. However, it remains unclear how the domain "knows" that it reached the correct state. After all, an intermediate state is not the minimum energy a state-the minimum is only expected for the whole structure. In the current geometric and thermodynamic approaches in protein folding mechanisms, impressive progress was made, as for instance exemplified by recent papers [4] [5], yet such bottom up approaches fail to provide a satisfactory and generally predictive solution.Munoz and Cerminara recently reviewed current generation of thermodynamic methods to map ultrafast folding landscapes, interaction networks and var...