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  • covalently
  • bR contains a covalently bound retinal chromophore that complicates unfolding analysis because it can slowly hydrolyze off in the SDS unfolded protein ( 12 ). (pnas.org)
  • binds
  • It also has large ramifications in both designing industrial processes where a protein is used to produce valuable products and in gauging how well a drug binds to its target (which will almost invariably itself be a protein). (london-nano.com)
  • For a drug to be effective it is important that it binds strongly to its protein target. (london-nano.com)
  • interactions
  • Mostly, these interactions will come into play spontaneously when cooling down the protein, thereby providing the active native conformation. (news-medical.net)
  • Interactions of the Major Cold Shock Protein of Bacillus subtilis CspB with Singlestranded DNA Templates of Different Base Composition'J. (nii.ac.jp)
  • methods
  • The overall agreement between predicted stability impact and experimental evidence for lower protein levels is in accordance with the estimated error rates of the methods. (proteopedia.org)
  • molecules
  • The development of the use of proteins, especially monoclonal antibodies (mAbs), as therapeutic molecules has provided many challenges. (selectscience.net)
  • The net contribution of an intramolecular hydrogen bond, an intermolecular one between protein and ordered water molecules, and an intermolecular one between ordered water molecules was estimated to be 8.5, 5.2, and 5.0 kJ/mol, respectively, for a hydrogen bond with 3 Å length. (nii.ac.jp)
  • slowly
  • The LCN study, published in Nature: scientific reports , shows that the stability of protein can be measured by slowly subjecting it to an increasing amount of heat, delivered by an Infrared laser beam in a ultra-small volume glass tube, replicating the conditions found within the bioreactors of industrial processes. (london-nano.com)
  • When cells receive Wnt, it's a signal for them to degrade their proteins more slowly, to keep them for a longer period of time because they're needed to regulate certain cell functions, such as proliferation. (healthcanal.com)
  • typically
  • The amine compounds mainly suppress chemical modification, typically the β-elimination of disulfide bond and deamidation of asparagine side chain, thereby preventing heat-induced inactivation of proteins. (eurekaselect.com)
  • concentration
  • The fraction unfolded, however, can be accurately measured only at high denaturant concentration, where the amount of unfolded protein is large enough-the so-called transition zone. (pnas.org)
  • Hi, I am abit new to the field but I suggest for stability check the protein concentration after some times and see how much is left. (protocol-online.org)
  • thermodynamics
  • DSC can also be used to measure the extent to which the stability and thermodynamics are affected by the simple effects associated with variations in protonation of macromolecules. (news-medical.net)
  • temperatures
  • Two of the variants, Thr 26-->Ser (T26S) and Thr 151-->Ser (T151S), have increased reversible melting temperatures with respect to the wild-type protein. (rcsb.org)