메뉴 건너뛰기




Volumn 58, Issue 9, 2001, Pages 1216-1233

How do thermophilic proteins deal with heat?

Author keywords

Adaptation; Electrostatics; Protein; Salt bridges; Structure; Temperature; Thermostability

Indexed keywords

AMINO ACID SEQUENCE; HEAT TRANSFER; NONHUMAN; PROTEIN CONFORMATION; PROTEIN STABILITY; REVIEW; TEMPERATURE SENSITIVITY; THERMOSTABILITY;

EID: 0034855858     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/PL00000935     Document Type: Review
Times cited : (393)

References (122)
  • 4
    • 0032092924 scopus 로고    scopus 로고
    • Extremophiles: Unusual and useful molecules are found in life on the edge of environmental tolerance
    • (1998) N. Biotechnol. , vol.16 , pp. 593-594
    • Persidis, A.1
  • 7
    • 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
  • 9
    • 0023959257 scopus 로고
    • Temperature adaptation of lactate dehydrogenase: Structural, functional and genetic aspects
    • (1988) Biophys. Chem. , vol.29 , pp. 171-179
    • Zuber, H.1
  • 16
    • 0029922615 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima: Strategies of protein stabilization
    • (1996) FEMS Microbiol. Rev. , vol.18 , pp. 215-224
    • Jaenicke, R.1
  • 22
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey
    • (2000) Structure , vol.8 , pp. 493-504
    • Szilagyi, A.1    Zavodszky, P.2
  • 67
    • 0030699086 scopus 로고    scopus 로고
    • Methionine aminopeptidase from the hyperthermophile archaeon Pyrococcus furiosus: Molecular cloning and overexpression in E. coli of the gene and characteristics of the enzyme
    • (1997) J. Biochem. , vol.122 , pp. 843-850
    • Tsunasawa, S.1    Izu, Y.2    Miyagi, M.3    Kato, I.4
  • 85
    • 0034161476 scopus 로고    scopus 로고
    • Protein-length distributions for the three domains of life
    • (2000) Trends Genet. , vol.16 , pp. 107-109
    • Zhang, J.1
  • 90
    • 0034561026 scopus 로고    scopus 로고
    • Fluctuations between stabilizing and destabilizing electrostatic contributions of ion pairs in conformers of the c-Myc-Max leucine zipper
    • (2000) Proteins , vol.41 , pp. 485-497
    • Kumar, S.1    Nussinov, R.2
  • 91
    • 0035371061 scopus 로고    scopus 로고
    • Ion pairs and their stabilities fluctuate in NMR conformer ensembles of proteins
    • (2001) Proteins , vol.43 , pp. 433-454
    • Kumar, S.1    Nussinov, R.2
  • 94
    • 0028574137 scopus 로고
    • Contribution of a hydrogen bond/salt bridge network to the stability of secondary and tertiary structures in lambda repressor
    • (1994) Protein Sci. , vol.3 , pp. 2217-2225
    • Marqusee, S.1    Sauer, R.T.2
  • 101
    • 0031003188 scopus 로고    scopus 로고
    • Contribution of a salt bridge to the thermostability of DNA binding protein HU from Bacillus stearothermophilus determined by site directed mutagenesis
    • (1997) J. Biochem. , vol.121 , pp. 448-455
    • Kawamura, S.1    Tanaka, I.2    Kimura, M.3
  • 102
    • 0029936488 scopus 로고    scopus 로고
    • Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 2.5Å resolution
    • (1996) Biochemistry , vol.35 , pp. 2597-2609
    • Tanner, J.J.1    Hecht, R.M.2    Krause, K.L.3
  • 110
    • 0032573431 scopus 로고    scopus 로고
    • The stability of salt bridges at high temperatures: Implications for hyperthermophilic proteins
    • (1998) J. Mol. Biol. , vol.284 , pp. 489-502
    • Elcock, A.H.1
  • 111


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.