Thermodynamic analysis of the effect of selective monodeamidation at asparagine 67 in ribonuclease A.

scientific article published on August 1997

Thermodynamic analysis of the effect of selective monodeamidation at asparagine 67 in ribonuclease A. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1002/PRO.5560060808
P932PMC publication ID2143771
P698PubMed publication ID9260280
P5875ResearchGate publication ID13960504

P50authorSante CapassoQ67548482
P2093author name stringBarone G
Graziano G
Catanzano F
P2860cites workStructure of phosphate-free ribonuclease A refined at 1.26 .ANGQ27728590
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Sequence-specific deamidation: isolation and biochemical characterization of succinimide intermediates of recombinant hirudin.Q54249569
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DSC Study of the Thermal Stability of S-Protein and S-Peptide/S-Protein Complexes†Q57956541
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Selective deamidation of ribonuclease A. Isolation and characterization of the resulting isoaspartyl and aspartyl derivativesQ70589335
The observed change in heat capacity accompanying the thermal unfolding of proteins depends on the composition of the solution and on the method employed to change the temperature of unfoldingQ71017334
Heterogeneity of bovine seminal ribonucleaseQ71033279
P433issue8
P407language of work or nameEnglishQ1860
P304page(s)1682-1693
P577publication date1997-08-01
P1433published inProtein ScienceQ7251445
P1476titleThermodynamic analysis of the effect of selective monodeamidation at asparagine 67 in ribonuclease A
P478volume6

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cites work (P2860)
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