![]() Joseph’s College in Trichy. In 1942, Ramachandran stood first in the B.Sc (Hons), Physics and was admitted to the Indian Institute of Science (IISc), Bengaluru, to study electrical engineering. Narayana Iyer, a Professor of Mathematics at Maharaja’s College, Ernakulam. Ramachandran stood first in the Intermediate examination and was admitted to St. Gopalasamudram Narayana Ramachandran was born to G.R. The story of this deprived genius, known as GNR among friends and students who went through painful illness in the last years of his life, needs to be told. Ramachandran on October 8, 2022, there appears to be very little enthusiasm to remember this giant of the Indian Science. As we celebrate the birth centenary of G.N. One name which should have figured along with them seems to be forgotten. Information from the present study arising from the synchrotron-based IR probing of the protein secondary structures of protein sources at the cellular level will be valuable as a guide to maintaining protein quality and predicting digestive behaviours.The city of Chennai has produced luminaries in field of science like C.V. Further study is needed to determine the sensitivities of protein secondary structures to various heat-processing conditions, and to quantify the relationship between protein secondary structures and the nutrient availability and digestive behaviour of various protein sources. The present results demonstrate the potential of highly spatially resolved synchrotron-based infrared microspectroscopy to locate 'pure' protein in feed tissues, and reveal protein secondary structures and digestive behaviour, making a significant step forward in and an important contribution to protein nutritional research. These results were proved by the Cornell Net Carbohydrate Protein System in situ animal trial, which also revealed that roasting increased the amount of protein bound to lignin, and well as of the Maillard reaction protein (both of which are poorly used by ruminants), and increased the level of indigestible and undegradable protein in ruminants. It is found that the semiclassical ansatz is a poor approximation, while the more sophisticated -sheet ratio (from 0.3 to 0.7) in the golden flaxseeds, which indicated a negative effect of the roasting on protein values, utilisation and bioavailability. The quality of these states for an approximate solution of the time-dependent Schroedinger equation is investigated. Results as obtained with the usually used ansaetze are discussed. This mechanism is based on a coupling of amide-I oscillators to acoustic phonons in a hydrogen bonded chain. The mechanism for energy and signal transport in proteins is suggested by Davydov is discussed. Our results are compatible with the soliton model of protein folding and provide first insight into soliton-formation dynamics. We analyzed 80 ns trajectories, obtained with one united-atom and two different all-atom force fields, to justify the side-chain orientation quantification scheme adopted in the studies and to eliminate force-field based artifacts. We performed in silico experiments for unfolding one subunit of the core structure of gp41 from the HIV envelope glycoprotein (PDB ID: 1AIK ) by molecular-dynamics simulations with the MD package GROMACS. The soliton manifestation is the pattern helix–loop–helix in the secondary structure of the protein, which explains the importance of understanding loop formation in helical proteins. Here we study the dynamics of this process by means of molecular-dynamics simulations. Soliton solutions of a generalized discrete non-linear Schrödinger equation (GDNLSE) obtained from the energy function in terms of bond and torsion angles κ and τ provide a constructive theoretical framework for describing protein folds and folding patterns. Furthermore, a wrong fold is a common cause for a protein to lose its function or even endanger the living organism. The protein-folding problem endures as one of the most important unresolved more » problems in science it addresses the origin of life itself. Despite the progress in understanding the process rate and the success in folding prediction for some small proteins, with presently available physics-based methods it is not yet possible to reliably deduce the shape of a biologically active protein from its amino acid sequence. Anfinsen’s dogma states that the native 3D shape of a protein is completely determined by protein’s amino acid sequence. Protein folding is the process of formation of a functional 3D structure from a random coil - the shape in which amino-acid chains leave the ribosome. ![]()
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