Solution structure and thermal stability of ribosomal protein L30e from hyperthermophilic archaeon Thermococcus celer

Protein Science

Volumn 12, Issue 7, 2003, Pages 1483-1495

  Wong, Kam Bo ^a   Lee, Chi Fung ^a   Chan, Siu Hong ^a   Leung, Tak Yuen ^a   Chen, Yu Wai ^b   Bycroft, Mark ^b  

^a CHINESE UNIVERSITY OF HONG KONG   (Hong Kong)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Helix capping; NMR; Protein structure; Ribosome; RNA binding

Indexed keywords

PROLINE; RIBOSOME PROTEIN; RIBOSOME PROTEIN L30E; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; ELECTRICITY; HYDROGEN BOND; MELTING POINT; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE; THERMOCOCCUS; THERMOCOCCUS CELER; THERMOSTABILITY; YEAST;

AMINO ACID SEQUENCE; ARCHAEAL PROTEINS; BINDING SITES; HEAT; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PHASE TRANSITION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; RIBOSOMAL PROTEINS; SEQUENCE ALIGNMENT; SOLUTIONS; THERMOCOCCUS; THERMODYNAMICS;

ARCHAEA; BACTERIA (MICROORGANISMS); THERMOCOCCUS; THERMOCOCCUS CELER;

EID: 0037972269     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0302303     Document Type: Article

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