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Volumn 157, Issue 2, 2002, Pages 178-180

Hydrogen bonds in human ubiquitin reflected in temperature coefficients of amide protons

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE; UBIQUITIN;

EID: 0036386164     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmre.2002.2597     Document Type: Article
Times cited : (74)

References (13)
  • 1
    • 0030858227 scopus 로고    scopus 로고
    • Extracting information from the temperature gradients of polypeptide HN chemical shifts. 1. The importance of conformational averaging
    • N.H. Andersen J.W. Neidigh S.M. Harris G.M. Lee Z. Liu H. Tong Extracting information from the temperature gradients of polypeptide HN chemical shifts. 1. The importance of conformational averaging J. Am. Chem. Soc. 119 1997 8547 8561
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 8547-8561
    • Andersen, N.H.1    Neidigh, J.W.2    Harris, S.M.3    Lee, G.M.4    Liu, Z.5    Tong, H.6
  • 2
    • 0034129479 scopus 로고    scopus 로고
    • NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): Structural similarity with Ascaris protease inhibitors
    • T. Cierpicki J. Bania J. Otlewski NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): Structural similarity with Ascaris protease inhibitors Protein Sci. 9 2000 976 984
    • (2000) Protein Sci. , vol.9 , pp. 976-984
    • Cierpicki, T.1    Bania, J.2    Otlewski, J.3
  • 3
    • 0034613028 scopus 로고    scopus 로고
    • Determination of a high precision structure of a novel protein, Linum usitatissimum trypsin inhibitor (LUTI), using computer-aided assignment of NOESY cross-peaks
    • T. Cierpicki J. Otlewski Determination of a high precision structure of a novel protein, Linum usitatissimum trypsin inhibitor (LUTI), using computer-aided assignment of NOESY cross-peaks J. Mol. Biol. 302 2000 1179 1192
    • (2000) J. Mol. Biol. , vol.302 , pp. 1179-1192
    • Cierpicki, T.1    Otlewski, J.2
  • 4
    • 0031160103 scopus 로고    scopus 로고
    • Temperature dependence of 1H chemical shifts in proteins
    • N.J. Baxter M.P. Williamson Temperature dependence of 1H chemical shifts in proteins J. Biomol. NMR 9 1997 359 369
    • (1997) J. Biomol. NMR , vol.9 , pp. 359-369
    • Baxter, N.J.1    Williamson, M.P.2
  • 5
    • 0035215289 scopus 로고    scopus 로고
    • Amide proton temperature coefficients as hydrogen bond indicators in proteins
    • T. Cierpicki J. Otlewski Amide proton temperature coefficients as hydrogen bond indicators in proteins J. Biomol. NMR 21 2001 249 261
    • (2001) J. Biomol. NMR , vol.21 , pp. 249-261
    • Cierpicki, T.1    Otlewski, J.2
  • 6
    • 0032528033 scopus 로고    scopus 로고
    • Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase
    • G. Cornilescu J.L. Marquardt M. Ottiger A. Bax Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase J. Am. Chem. Soc. 120 1998 6836 6837
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 6836-6837
    • Cornilescu, G.1    Marquardt, J.L.2    Ottiger, M.3    Bax, A.4
  • 7
    • 0000865993 scopus 로고
    • A new analysis of proton chemical shifts in proteins
    • K. Osapay D.A. Case A new analysis of proton chemical shifts in proteins J. Am. Chem. Soc. 113 1991 9436 9444
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 9436-9444
    • Osapay, K.1    Case, D.A.2
  • 9
    • 0033620446 scopus 로고    scopus 로고
    • Identification of the hydrogen bonding network in a protein by scalar couplings
    • G. Cornilescu J.S. Hu A. Bax Identification of the hydrogen bonding network in a protein by scalar couplings J. Am. Chem. Soc. 121 1999 2949 2950
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2949-2950
    • Cornilescu, G.1    Hu, J.S.2    Bax, A.3
  • 10
    • 0002352277 scopus 로고    scopus 로고
    • Temperature coefficients of peptides dissolved in hexafluoroisopropanol monitor distortions of helices
    • M.A. Contreras T. Haack M. Royo E. Giralt M. Pons Temperature coefficients of peptides dissolved in hexafluoroisopropanol monitor distortions of helices Lett. Pept. Sci. 4 1997 29 39
    • (1997) Lett. Pept. Sci. , vol.4 , pp. 29-39
    • Contreras, M.A.1    Haack, T.2    Royo, M.3    Giralt, E.4    Pons, M.5
  • 11
    • 33845552240 scopus 로고
    • Hydrogen bond length and 1H NMR chemical shifts in proteins
    • G. Wagner A. Pardi K. Wüthrich Hydrogen bond length and 1H NMR chemical shifts in proteins J. Am. Chem. Soc. 1983 1983 5948 5949
    • (1983) J. Am. Chem. Soc. , vol.1983 , pp. 5948-5949
    • Wagner, G.1    Pardi, A.2    Wüthrich, K.3
  • 13
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • R. Koradi M. Billeter K. Wüthrich MOLMOL: A program for display and analysis of macromolecular structures J. Mol. Graph. 14 1996 51 55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.