By Feng Gai, Deguo Du, Yao Xu (auth.), Yawen Bai, Ruth Nussinov (eds.)
Protein Folding Protocols offers protocols for learning and characterizing protein folding from the spread out to the folded kingdom. overlaying test and conception, bioinformatics methods, and state of the art simulation protocols for larger sampling of the conformational house, this quantity describes a wide diversity of strategies to check, expect, and research the protein folding method.
Protein Folding Protocols additionally offers pattern methods towards the prediction of protein constitution ranging from the amino acid series, within the absence of total homologous sequences. those methods have super implications, starting from drug layout, practical project, comprehension of the character of law, knowing molecular machines, viral access into cells, and placing jointly mobile pathways and their dynamics.
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Extra resources for Protein Folding Protocols
The latter group (19) developed pressure-resisting cells (Fig. 2) made up initially of glass, then of quartz (both hand-made) (23), and used them on a commercial NMR probe. This is the on-line cell high-pressure NMR system described in some detail in the following section. Although the inner space of the pressure-resistive cell is so small (typically ~20 µL; Fig. 2) that the signal intensity is inherently low, the field homogeneity can be extremely good and allows all two- or multidimensional spectral measurements, giving 24 Lassalle and Akasaka excellent high resolution multidimensional spectra as those obtained with normal 5-mm tubes at 1 bar.
The basic equations governing the stability of proteins on the p and/or T axes are given in the following: 1. By taking the pressure dependence of ∆G to the first order at constant temperature, ∆G = ∆G1obar + p∆V 0 (1) and to the second order, ∆G p − ∆G o = ∆V 0 ( p − po ) − ∆β ( p − po )2 2 (1′) 2. By taking the “exact” expression for temperature dependence of ∆G and the pressure dependence of ∆G to the second order, ⎡ ⎛ T ⎤ ⎞ ∆G = ∆G o − ∆S o (T – T 0 ) – ∆C p ⎢T ⎝ ln o – 1⎠ + T o ⎥ T ⎣ ⎦ + ∆V o ( p – p o ) − ∆β ( p – p o )2 + ∆α ( p – p o )(T – T o ) 2 (2) Performing a Taylor expansion and neglecting higher order terms with respect to temperature, this equation equals the following: 26 Lassalle and Akasaka G = ∆G o – ∆ S o (T – T 0 ) – − ∆C p 2T o (T – T o )2 + ∆V o ( p – p o ) (2′) ∆β ( p – p o )2 + ∆α ( p – p o )(T – T o ) 2 Utilizing Eq.
Index. METHODS IN MOLECULAR BIOLOGY ™ 350 Protein Folding Protocols Edited by Yawen Bai Ruth Nussinov 2 The Use of High-Pressure Nuclear Magnetic Resonance to Study Protein Folding Michael W. Lassalle and Kazuyuki Akasaka Summary Recent development of high-pressure cells for a variety of spectroscopic methods has enabled the use of pressure as one of the commonly used perturbations along with temperature and chemical perturbations to study folding/unfolding reactions of proteins. Although various high-pressure spectroscopy techniques have their own significance, high-pressure nuclear magnetic resonance (NMR) is unique in that it allows one to gain residue-specific and atom-detailed information from proteins under pressure.
Protein Folding Protocols by Feng Gai, Deguo Du, Yao Xu (auth.), Yawen Bai, Ruth Nussinov (eds.)