机译:末端二硫键在巴西甜味剂甜度中的结构作用
Department of Chemistry, University of Wisconsin-Madison, 1101 University Drive, Madison, WI 53706, USA;
Biochemistry Department, University of Wisconsin-Madison, 433 Babcock Drive, Madison, WI 53706, USA;
National Magnetic Resonance Facility at Madison, University of Wisconsin-Madison, 433 Babcock Drive, Madison, WI 53706, USA;
Department of Pharmacology, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA;
Biochemistry Department, University of Wisconsin-Madison, 433 Babcock Drive, Madison, WI 53706, USA|National Magnetic Resonance Facility at Madison, University of Wisconsin-Madison, 433 Babcock Drive, Madison, WI 53706, USA;
Department of Neuroscience, Mount Sinai School of Medicine, 1 Gustave Levy Place, New York, NY 10029, USA;
机译:末端二硫键在巴西甜味剂甜度中的结构作用
机译:甜蛋白巴西青素中二硫键的分配
机译:高效,快速的蛋白质表达和纯化含有高二硫键的甜蛋白brazzein在大肠杆菌中的表达
机译:通过ESI-LTQ-orbitrap-MS分析的层粘连蛋白β1和γ1N末端构建体的二硫键图案
机译:免疫球蛋白轻链的折叠:解折叠和重新折叠的机理,链内二硫键的作用以及二硫键形成的机理
机译:末端二硫键在巴西甜味剂甜度中的结构作用
机译:人血纤蛋白原变体的自然发生破坏了链间二硫键(AαCys36Gly,AαCys36Arg和AαCys45Tyr),证实了N末端A {α}二硫键在蛋白质组装和分泌中的作用。