I. Study of protein aggregation due to heat denaturation: A structural approach using circular dichroism spectroscopy, nuclear magnetic resonance, and static light scattering

Biotechnology and Bioengineering

Volumn 59, Issue 3, 1998, Pages 273-280

  Tsai, Amos M ^a,b   Van Zanten, John H ^a   Betenbaugh, Michael J ^a  

^a Johns Hopkins University   (United States)

^b UNIVERSITY OF MARYLAND BIOTECHNOLOGY INSTITUTE   (United States)

Author keywords

Heat denaturation; Protein aggregation; RNase A

Indexed keywords

ENZYMES; LIGHT SCATTERING; MOLECULAR ORIENTATION; MOLECULAR STRUCTURE; MOLECULES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; TEMPERATURE;

CHARGE-CHARGE REPULSION; CIRCULAR DICHROISM SPECTROSCOPY; HEAT DENATURATION; MELTING TEMPERATURE; PROTEIN AGGREGATION; RNASE A; STATIC LIGHT SCATTERING;

BIOTECHNOLOGY;

RIBONUCLEASE A;

ARTICLE; CIRCULAR DICHROISM; ENZYME DENATURATION; ENZYME STABILITY; LIGHT SCATTERING; NUCLEAR MAGNETIC RESONANCE; PH; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTON TRANSPORT;

CIRCULAR DICHROISM; HEAT; HYDROGEN-ION CONCENTRATION; LIGHT; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN DENATURATION; RIBONUCLEASE, PANCREATIC; SCATTERING, RADIATION; THERMODYNAMICS;

EID: 0032486770     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19980805)59:3<273::AID-BIT2>3.0.CO;2-8     Document Type: Article

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