Studies on the structure of mouse helix-destabilizing protein-1. DNA binding and controlled proteolysis with trypsin.

Medicine & Life Sciences

• Mouse Hnrnpa1 protein 100%
• Trypsin 43%
• Proteolysis 39%
• Single-Stranded DNA 35%
• Proteins 15%
• helix-destabilizing proteins 13%
• DNA-cellulose 10%
• Digestion 8%
• Cellulose 7%
• 2'-deoxythymidylyl-(3'-5')-2'-deoxyadenosine 5%
• poly A-T 5%
• Molecular Weight 5%
• Poly T 5%
• Binding Sites 4%
• Polynucleotides 4%
• High Mobility Group Proteins 4%
• Peptide Mapping 4%
• Dextran Sulfate 3%
• Isoelectric Focusing 3%
• Tryptophan 3%
• Thymus Gland 3%
• Histones 3%
• Hydrolysis 2%
• Chromatin 2%
• Carrier Proteins 2%
• Fluorescence 2%
• Nucleotides 2%

Chemical Compounds

• Protein Hydrolysis 45%
• Trypsin 39%
• Single-Stranded DNA 39%
• Protein 17%
• Nucleotide Residue 8%
• Binding Site 7%
• Subcellular Localization 7%
• Dextran Sulfate 7%
• Peptide Mapping 6%
• Polynucleotide 5%
• Isoelectric Focusing 5%
• Histone 5%
• Weight 5%
• Sedimentation 5%
• Tryptophan 4%
• Compound Mobility 4%
• Hydrolysis 3%
• Fluorescence 3%
• Molecule 1%