title: Heated proteins are still active in a functionalized nanoporous support.
abstract: Even under heated conditions, the nearly native conformation and activity of a protein can be hoarded in a functionalized nanoporous support via non-covalent interaction. Surprisingly, the protein released from the heated protein-nanoporous composite can maintain its nearly native conformation and activity, while free proteins are permanently denatured under the same treatment.
authors: Pacific Northwest National Laboratory, PO Box 999, Richland, WA 99352, USA.
authors: Baowei
authors: B
authors: Chen
authors: Wen
authors: W
authors: Qi
authors: Xiaolin
authors: X
authors: Li
authors: Chenghong
authors: C
authors: Lei
authors: Jun
authors: J
authors: Liu
mesh_terms: D005949:Glucose Oxidase / Q000378:metabolism*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D058608:Nanopores / Q000648:ultrastructure; D016062:Porosity; D011487:Protein Conformation; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D012822:Silicon Dioxide / Q000737:chemistry; D013050:Spectrometry, Fluorescence
chemical_list: D011506:Proteins; D012822:Silicon Dioxide; D005949:Glucose Oxidase
keywords: glucose oxidase; mesoporous silica; protein denaturation; protein release