Electrophoretic analysis of the unfolding of proteins by urea.
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Solution Structure of the Monovalent Lectin Microvirin in Complex with ManĀ (1-2)Man Provides a Basis for Anti-HIV Activity with Low ToxicityArthrobacter D-xylose isomerase: partial proteolysis with thermolysin.Polypeptide binding properties of the chaperone calreticulin.Dimerization and oligomerization of the chaperone calreticulin.Reexamination of alcohol dehydrogenase structural mutants in Drosophila using protein blottingRole of proline isomerization in folding of ribonuclease A at low temperaturesConstruction of heterodimer tyrosyl-tRNA synthetase shows tRNATyr interacts with both subunitsEF-hand proteins and the regulation of actin-myosin interaction in the eutardigrade Hypsibius klebelsbergi (tardigrada).Purification of the 300K intermediate filament-associated protein and its in vitro recombination with intermediate filaments.Elucidating the early stages of keratin filament assemblyEarly events in the disulfide-coupled folding of BPTI.Purification and properties of a fifth major viral gag protein from avian sarcoma and leukemia virusesImmunological relationship between anionic antimicrobial proteins from caries-free individuals and known salivary antimicrobial factors.Extracellular superoxide dismutase exists as an octamer.Protein complexes of intermediate-sized filaments: melting of cytokeratin complexes in urea reveals different polypeptide separation characteristics.Self crowding of globular proteins studied by small-angle x-ray scattering.Minimal effects of macromolecular crowding on an intrinsically disordered protein: a small-angle neutron scattering study.Amino-acid substitutions at the fully exposed P1 site of bovine pancreatic trypsin inhibitor affect its stability.Metal-ion binding and the molecular conformational properties of alpha lactalbumin.Isoforms of green fluorescent protein differ from each other in solvent molecules 'trapped' inside this protein.Biochemical characterization of Porphyromonas (Bacteroides) gingivalis collagenase.Adenosine dimethylation of 16S ribosomal RNA: effect of the methylgroups on local conformational stability as deduced from electrophoretic mobility of RNA fragments in denaturing polyacrylamide gels.Destabilization of secondary structure in 16S ribosomal RNA by dimethylation of two adjacent adenosines.Preparative isolation of the two forms of pig pancreatic pro-(carboxypeptidase A) and their monomeric carboxypeptidases AStability of mutant actins.1H-n.m.r. studies of the isolated activation segment from pig procarboxypeptidase A.The electrophoresis of transferrins in urea/polyacrylamide gels.Glucosamine-6-phosphate deaminase from Escherichia coli has a trimer of dimers structure with three intersubunit disulphidesStability of Arthrobacter D-xylose isomerase to denaturants and heat.Size is a major determinant of dissociation and denaturation behaviour of reconstituted high-density lipoproteins.Human serum amyloid A protein. Behaviour in aqueous and urea-containing solutions and antibody production.Refolding human serum albumin at relatively high protein concentration.Transverse urea-gradient gel electrophoresis.Chaperonin GroEL reassembly: an effect of protein ligands and solvent composition.Association of the radiosensitizers metronidazole and misonidazole (RO-07-0582) with bovine serum albumin. Effect of urea and ionic strength.Amino acid substitutions at the subunit interface of dimeric Escherichia coli alkaline phosphatase cause reduced structural stability.Arthrobacter D-xylose isomerase: protein-engineered subunit interfaces.Conformational stability of pGEX-expressed Schistosoma japonicum glutathione S-transferase: a detoxification enzyme and fusion-protein affinity tag.Interaction with magnesium and ADP stabilizes both components of nitrogenase from Klebsiella pneumoniae against urea denaturation.Selective reduction of a disulphide bridge in hen ovotransferrin.
P2860
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P2860
Electrophoretic analysis of the unfolding of proteins by urea.
description
1979 nĆ® lÅ«n-bĆ»n
@nan
1979幓ć®č«ę
@ja
1979幓č«ę
@yue
1979幓č«ę
@zh-hant
1979幓č«ę
@zh-hk
1979幓č«ę
@zh-mo
1979幓č«ę
@zh-tw
1979幓č®ŗę
@wuu
1979幓č®ŗę
@zh
1979幓č®ŗę
@zh-cn
name
Electrophoretic analysis of the unfolding of proteins by urea.
@en
type
label
Electrophoretic analysis of the unfolding of proteins by urea.
@en
prefLabel
Electrophoretic analysis of the unfolding of proteins by urea.
@en
P1476
Electrophoretic analysis of the unfolding of proteins by urea.
@en
P2093
Creighton TE
P304
P356
10.1016/0022-2836(79)90279-1
P407
P577
1979-04-01T00:00:00Z