메뉴 건너뛰기




Volumn 297, Issue 4, 2000, Pages 975-988

Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticus cold shock protein

Author keywords

Atomic resolution crystal structure; Bacillus caldolyticus; Cold shock protein; Electrostatic interactions; Thermal Stability

Indexed keywords

COLD SHOCK PROTEIN;

EID: 0034615784     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3602     Document Type: Article
Times cited : (111)

References (57)
  • 4
  • 5
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 36
    • 0016771835 scopus 로고
    • Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2
    • (1975) Nature , vol.255 , pp. 256-259
    • Perutz, M.1    Raidt, H.2
  • 38
    • 0031776135 scopus 로고    scopus 로고
    • Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: A practical guide to recognizing and interpreting polyelectrolyte effects, Hofmeister effects and osmotic effects of salts
    • (1998) Adv. Protein Chem. , vol.51 , pp. 281-353
    • Record, M.T.1    Zhang, W.2    Anderson, C.F.3
  • 41
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 50
    • 85031601860 scopus 로고    scopus 로고
    • Struktur-Funktionsbeziehungen und Regulation des Hauptkalteschock-Proteins CspB aus Bacillus subtilis. PhD thesis, Marburg University, Germany
    • (1996)
    • Schroder, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.