Conformational stability of globular proteins

Conformational stability of globular proteins

The conformational stability of ribonuclease T 1 has been measured as a function of the variables of most interest to biochemists: temperature, pH, salt concentration, disulfide-bond content and amino acid sequence. The results provide insight into the forces that stabilize globular proteins.

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Bibliographische Detailangaben
Veröffentlicht in:Trends in Biochemical Sciences 1990, Vol.15 (1), p.14-17
1. Verfasser: Pace, C.Nick
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acid Sequence
Endoribonucleases
Isoelectric Point
Molecular Sequence Data
Protein Conformation
Ribonuclease T1
Thermodynamics
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Beschreibung
Zusammenfassung:The conformational stability of ribonuclease T 1 has been measured as a function of the variables of most interest to biochemists: temperature, pH, salt concentration, disulfide-bond content and amino acid sequence. The results provide insight into the forces that stabilize globular proteins.
ISSN:0968-0004
1362-4326
DOI:10.1016/0968-0004(90)90124-T