Utilization of Methyl Proton Resonances in Cross-Saturation Measurement for Determining the Interfaces of Large Protein–Protein Complexes

[1]  F. Dahlquist,et al.  The contact interface of a 120 kD CheA-CheW complex by methyl TROSY interaction spectroscopy. , 2005, Journal of the American Chemical Society.

[2]  D. Wyss,et al.  Sequence-specific assignments of methyl groups in high-molecular weight proteins. , 2004, Journal of the American Chemical Society.

[3]  Y. Fukunishi,et al.  The Filling Potential Method: A Method for Estimating the Free Energy Surface for Protein−Ligand Docking , 2003 .

[4]  L. Kay,et al.  Ile, Leu, and Val methyl assignments of the 723-residue malate synthase G using a new labeling strategy and novel NMR methods. , 2003, Journal of the American Chemical Society.

[5]  L. Kay,et al.  Methyl TROSY: explanation and experimental verification , 2003 .

[6]  L. Kay,et al.  Cross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes. , 2003, Journal of the American Chemical Society.

[7]  L. Kay,et al.  Side chain assignments of Ile delta 1 methyl groups in high molecular weight proteins: an application to a 46 ns tumbling molecule. , 2003, Journal of the American Chemical Society.

[8]  R. Nussinov,et al.  Protein–protein interactions: Structurally conserved residues distinguish between binding sites and exposed protein surfaces , 2003, Proceedings of the National Academy of Sciences of the United States of America.

[9]  G. Wider,et al.  Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelles , 2002, Journal of biomolecular NMR.

[10]  F. Löhr,et al.  Correlation of backbone amide and side-chain (13)C resonances in perdeuterated proteins. , 2002, Journal of magnetic resonance.

[11]  I. Shimada,et al.  Determination of the interface of a large protein complex by transferred cross-saturation measurements. , 2002, Journal of molecular biology.

[12]  N. Krishna,et al.  Complete relaxation and conformational exchange matrix (CORCEMA) analysis of intermolecular saturation transfer effects in reversibly forming ligand-receptor complexes. , 2002, Journal of magnetic resonance.

[13]  A. Lane,et al.  Determining binding sites in protein–nucleic acid complexes by cross-saturation , 2001, Journal of biomolecular NMR.

[14]  Renaldo Mendoza,et al.  NMR-Based Screening of Proteins Containing 13C-Labeled Methyl Groups , 2000 .

[15]  R. Nussinov,et al.  Conservation of polar residues as hot spots at protein interfaces , 2000, Proteins.

[16]  E. Eisenmesser,et al.  Accuracy of bound peptide structures determined by exchange transferred nuclear Overhauser data: A simulation study , 2000, Journal of biomolecular NMR.

[17]  Hideo Takahashi,et al.  A novel NMR method for determining the interfaces of large protein–protein complexes , 2000, Nature Structural Biology.

[18]  L. Kay,et al.  A robust and cost-effective method for the production of Val, Leu, Ile (δ1) methyl-protonated 15N-, 13C-, 2H-labeled proteins , 1999, Journal of biomolecular NMR.

[19]  C. Chothia,et al.  The atomic structure of protein-protein recognition sites. , 1999, Journal of molecular biology.

[20]  H. Senn,et al.  Fast-HMQC using Ernst angle pulses: An efficient tool for screening of ligand binding to target proteins , 1997, Journal of biomolecular NMR.

[21]  M. Billeter,et al.  MOLMOL: a program for display and analysis of macromolecular structures. , 1996, Journal of molecular graphics.

[22]  E. Kupče,et al.  Wideband Homonuclear Decoupling in Protein Spectra , 1995 .

[23]  S. Grzesiek,et al.  NMRPipe: A multidimensional spectral processing system based on UNIX pipes , 1995, Journal of biomolecular NMR.

[24]  I. Shimada,et al.  Three-dimensional solution structure of the B domain of staphylococcal protein A: comparisons of the solution and crystal structures. , 1992, Biochemistry.

[25]  A. Bax,et al.  Resolution enhancement and spectral editing of uniformly 13C-enriched proteins by homonuclear broadband 13C decoupling , 1992 .

[26]  G. Wider,et al.  Studies of slow conformational equilibria in macromolecules by exchange of heteronuclear longitudinal 2-spin-order in a 2D difference correlation experiment , 1991 .

[27]  R. Ishima,et al.  General features of proton longitudinal relaxation in proteins in solution , 1991 .

[28]  I. Shimada,et al.  Sequential 1H NMR assignments and secondary structure of the B domain of staphylococcal protein A: structural changes between the free B domain in solution and the Fc-bound B domain in crystal. , 1990, Biochemistry.

[29]  Kurt Wüthrich,et al.  Stereospecific assignment of the methyl 1H NMR lines of valine and leucine in polypeptides by nonrandom 13C labelling , 1989 .

[30]  L. Mueller.  Sensitivity enhanced detection of weak nuclei using heteronuclear multiple quantum coherence , 1979 .