메뉴 건너뛰기




Volumn 181, Issue 1, 2006, Pages 21-28

Alanine check points in HNN and HN(C)N spectra

Author keywords

Band selective pulse; Check points; HN(C)N A; HNN A; Triplets of residues

Indexed keywords

CORRELATION THEORY; GENES; NUCLEAR MAGNETIC RESONANCE; NUCLEIC ACID SEQUENCES; PROTEINS;

EID: 33745042221     PISSN: 10907807     EISSN: 10960856     Source Type: Journal    
DOI: 10.1016/j.jmr.2006.03.009     Document Type: Article
Times cited : (20)

References (25)
  • 3
    • 0000061511 scopus 로고
    • Carbon-13 line narrowing by deuterium decoupling in deuterium/carbon-13/nitrogen-15 enriched proteins. Application to triple resonance 4D J connectivity of sequential amides
    • Grzesiek S., Anglister J., Ren H., and Bax A. Carbon-13 line narrowing by deuterium decoupling in deuterium/carbon-13/nitrogen-15 enriched proteins. Application to triple resonance 4D J connectivity of sequential amides. J. Am. Chem. Soc. 115 (1993) 4369-4370
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 4369-4370
    • Grzesiek, S.1    Anglister, J.2    Ren, H.3    Bax, A.4
  • 4
    • 0030137565 scopus 로고    scopus 로고
    • Use of selective C alpha pulses for improvement of HN(CA)CO-D and HN(COCA)NH-D experiments
    • Matsuo H., Kupce E., Li H., and Wagner G. Use of selective C alpha pulses for improvement of HN(CA)CO-D and HN(COCA)NH-D experiments. J. Magn. Reson. B 111 (1996) 194-198
    • (1996) J. Magn. Reson. B , vol.111 , pp. 194-198
    • Matsuo, H.1    Kupce, E.2    Li, H.3    Wagner, G.4
  • 6
    • 0035846574 scopus 로고    scopus 로고
    • An efficient high-throughput resonance assignment procedure for structural genomics and protein folding research by NMR
    • Bhavesh N.S., Panchal S.C., and Hosur R.V. An efficient high-throughput resonance assignment procedure for structural genomics and protein folding research by NMR. Biochemistry 40 (2001) 14727-14735
    • (2001) Biochemistry , vol.40 , pp. 14727-14735
    • Bhavesh, N.S.1    Panchal, S.C.2    Hosur, R.V.3
  • 8
    • 0344413866 scopus 로고    scopus 로고
    • Structural characterization by NMR of the natively unfolded extracellular domain of beta-dystroglycan: toward the identification of the binding epitope for alpha-dystroglycan
    • Bozzi M., Bianchi M., Sciandra F., Paci M., Giardina B., Brancaccio A., and Cicero D.O. Structural characterization by NMR of the natively unfolded extracellular domain of beta-dystroglycan: toward the identification of the binding epitope for alpha-dystroglycan. Biochemistry 42 (2003) 13717-13724
    • (2003) Biochemistry , vol.42 , pp. 13717-13724
    • Bozzi, M.1    Bianchi, M.2    Sciandra, F.3    Paci, M.4    Giardina, B.5    Brancaccio, A.6    Cicero, D.O.7
  • 10
    • 0037031291 scopus 로고    scopus 로고
    • NMR identification and characterization of the flexible regions in the 160 kDa molten globule-like aggregate of barstar at low pH
    • Juneja J., Bhavesh N.S., Udgaonkar J.B., and Hosur R.V. NMR identification and characterization of the flexible regions in the 160 kDa molten globule-like aggregate of barstar at low pH. Biochemistry 41 (2002) 9885-9899
    • (2002) Biochemistry , vol.41 , pp. 9885-9899
    • Juneja, J.1    Bhavesh, N.S.2    Udgaonkar, J.B.3    Hosur, R.V.4
  • 12
    • 0041989754 scopus 로고    scopus 로고
    • A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex
    • Panchal S.C., Kaiser D.A., Torres E., Pollard T.D., and Rosen M.K. A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex. Nat. Struct. Biol. 10 (2003) 591-598
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 591-598
    • Panchal, S.C.1    Kaiser, D.A.2    Torres, E.3    Pollard, T.D.4    Rosen, M.K.5
  • 14
    • 23944444257 scopus 로고    scopus 로고
    • Clusters in an intrinsically disordered protein create a protein-binding site: the TolB-binding region of colicin E9
    • Tozawa K., Macdonald C.J., Penfold C.N., James R., Kleanthous C., Clayden N.J., and Moore G.R. Clusters in an intrinsically disordered protein create a protein-binding site: the TolB-binding region of colicin E9. Biochemistry 44 (2005) 11496-11507
    • (2005) Biochemistry , vol.44 , pp. 11496-11507
    • Tozawa, K.1    Macdonald, C.J.2    Penfold, C.N.3    James, R.4    Kleanthous, C.5    Clayden, N.J.6    Moore, G.R.7
  • 15
    • 20144365610 scopus 로고    scopus 로고
    • Structural and dynamic characterization of the acid-unfolded state of hUBF HMG box 1 provides clues for the early events in protein folding
    • Zhang X., Xu Y., Zhang J., Wu J., and Shi Y. Structural and dynamic characterization of the acid-unfolded state of hUBF HMG box 1 provides clues for the early events in protein folding. Biochemistry 44 (2005) 8117-8125
    • (2005) Biochemistry , vol.44 , pp. 8117-8125
    • Zhang, X.1    Xu, Y.2    Zhang, J.3    Wu, J.4    Shi, Y.5
  • 16
    • 0035999812 scopus 로고    scopus 로고
    • α coupling constants measured in J-modulated HSQCs
    • α coupling constants measured in J-modulated HSQCs. J. Biomol. NMR 23 (2002) 47-55
    • (2002) J. Biomol. NMR , vol.23 , pp. 47-55
    • Wirmer, J.1    Schwalbe, H.2
  • 18
    • 0030854651 scopus 로고    scopus 로고
    • Improved water and lipid suppression for 3D PRESS CSI using RF band selective inversion with gradient dephasing (BASING)
    • Star-Lack J., Nelson S.J., Kurhanewicz J., Huang L.R., and Vigneron D.B. Improved water and lipid suppression for 3D PRESS CSI using RF band selective inversion with gradient dephasing (BASING). Magn. Reson. Med. 38 (1997) 311-321
    • (1997) Magn. Reson. Med. , vol.38 , pp. 311-321
    • Star-Lack, J.1    Nelson, S.J.2    Kurhanewicz, J.3    Huang, L.R.4    Vigneron, D.B.5
  • 19
    • 0030900987 scopus 로고    scopus 로고
    • Design of adiabatic pulses for fat-suppression using analytic solutions of the Bloch equation
    • Rosenfeld D., Panfil S.L., and Zur Y. Design of adiabatic pulses for fat-suppression using analytic solutions of the Bloch equation. Magn. Reson. Med. 37 (1997) 793-801
    • (1997) Magn. Reson. Med. , vol.37 , pp. 793-801
    • Rosenfeld, D.1    Panfil, S.L.2    Zur, Y.3
  • 20
    • 3042565938 scopus 로고    scopus 로고
    • Broadband and band-selective IMPRESS-gHMBC: compensation of refocusing inefficiency with synchronized inversion sweep
    • Crouch R., Boyer R.D., Johnson R., and Krishnamurthy K. Broadband and band-selective IMPRESS-gHMBC: compensation of refocusing inefficiency with synchronized inversion sweep. Magn. Reson. Chem. 42 (2004) 301-307
    • (2004) Magn. Reson. Chem. , vol.42 , pp. 301-307
    • Crouch, R.1    Boyer, R.D.2    Johnson, R.3    Krishnamurthy, K.4
  • 21
    • 15844427294 scopus 로고    scopus 로고
    • A band-selective composite gradient: application to DQF-COSY
    • Bradley S.A., Hu H., Krishnamurthy K., and Hadden C.E. A band-selective composite gradient: application to DQF-COSY. J. Magn. Reson. 174 (2005) 110-115
    • (2005) J. Magn. Reson. , vol.174 , pp. 110-115
    • Bradley, S.A.1    Hu, H.2    Krishnamurthy, K.3    Hadden, C.E.4
  • 22
    • 4243461379 scopus 로고
    • Selective spin inversion in nuclear magnetic resonance and coherent optics through an exact solution of the Bloch-Riccati equation
    • Silver M.S., Joseph R.I., and Hoult D.I. Selective spin inversion in nuclear magnetic resonance and coherent optics through an exact solution of the Bloch-Riccati equation. Phys. Rev. A 31 (1985) 2753-2755
    • (1985) Phys. Rev. A , vol.31 , pp. 2753-2755
    • Silver, M.S.1    Joseph, R.I.2    Hoult, D.I.3
  • 23
    • 0035119625 scopus 로고    scopus 로고
    • Chemical shifts in denatured proteins: resonance assignments for denatured ubiquitin and comparisons with other denatured proteins
    • Peti W., Smith L.J., Redfield C., and Schwalbe H. Chemical shifts in denatured proteins: resonance assignments for denatured ubiquitin and comparisons with other denatured proteins. J. Biomol. NMR 19 (2001) 153-165
    • (2001) J. Biomol. NMR , vol.19 , pp. 153-165
    • Peti, W.1    Smith, L.J.2    Redfield, C.3    Schwalbe, H.4
  • 24
    • 0028170819 scopus 로고
    • DYNEINS: molecular structure and cellular function
    • Holzbaur E.L., and Vallee R.B. DYNEINS: molecular structure and cellular function. Annu. Rev. Cell Biol. 10 (1994) 339-372
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 339-372
    • Holzbaur, E.L.1    Vallee, R.B.2
  • 25
    • 0000968918 scopus 로고
    • Composite pulses for ultra broadband inversion
    • Shaka A.J. Composite pulses for ultra broadband inversion. Chem. Phys. Lett. 120 (1985) 201-205
    • (1985) Chem. Phys. Lett. , vol.120 , pp. 201-205
    • Shaka, A.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.