Conformational domains and structural transitions of human von Willebrand protein
作者： Joseph Loscalzo , Robert I. Handin
DOI: 10.1021/BI00312A014
关键词: Denaturation (biochemistry) 、 Circular dichroism 、 Protein structure 、 Guanidine 、 Fluorescence 、 Fluorescence spectrometry 、 Chemistry 、 Native state 、 Crystallography 、 Quenching (fluorescence)
摘要: The conformational states of human von Willebrand protein (vWF) were studied by using ultraviolet (UV) difference, circular dichroism, and fluorescence spectrophotometric techniques in order to gain insight into the forces that maintain its asymmetric, flexible shape. vWF has 24% alpha-helix 18% beta-pleated sheet structure native state. Disulfide bond reduction carboxamidation reduced content 50% without affecting alpha-helix. In addition, quantum yield intrinsic (tryptophan/tyrosine) decreased 33% after alkylation, affinity hydrophobic fluorescent probes 8-anilino-1-naphthalenesulfonate 6-(p-toluidino)-2-naphthalenesulfonate for was 2.5-fold. contrast, quenching acrylamide UV difference spectrum did not change following reduction. An analysis changes polarization emission maximum shift induced thermal guanidine hydrochloride denaturation revealed single, smooth transitions both vWF, suggesting existence an ordered species. This study shows (1) disulfide cause significant (2) may contain discrete, ordered, domains linked regions random polypeptide chain, (3) specific tertiary structural within are affected carboxamidation. model would explain asymmetry flexibility molecule.
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