116
B. BERSCH et al.: Protein Structure and Dynamics by NMR in Solution
Sattler M, Fesik SW (1996) Use of deuterium labeling in NMR: overcoming a sizeable problem. Structure 4: 1245-9.
Shuker SB, Hajduk pJ, Meadows RP, Fesik SW (1996) Discovering high-affinity ligands for proteins:
SAR by NMR. Science 274: 1531-1534.
Spera S, Bax A (1991) Empirical correlation between protein backbone conformation and C a and C~
l3C nuclear magnetic resonance chemical shifts J Am Chern Soc 1l3: 5490-5492.
Thielens NM, Aude CA, Lacroix MB, Gagnon J, Arlaud GJ (1990) Ca ' + binding properties and Ca ' +_
dependent interactions of the isolated N-terminal alpha fragments of human complement proteases C1r and CIs. J Bioi Chern 265, 14469-14475.
Thielens NM, Emie K, Lacroix M, Jaquinod M, Hernandez JF, Esser AF, Arlaud GF (1998) The
N-terminal CUB-EGF module pair of human complement protease C1r binds Ca ' + with high
affinity and mediates Ca'+-dependent interaction with CIs. J Bioi Chern 274: 9149-9159.
Tiede DM, Vashishta AC, Gunner MR (1993) Electron-transfer kinetics and electrostatic properties of
the Rhodobacter sphaeroides reaction center and soluble c cytochromes. Biochemistry 32:
4514-453l.
Tjandra N, Bax A (1997) Direct measurement of distances and angles in biomolecules by NMR in a
dilute liquid crystalline medium. Science 278: 1111- 1114.
Tjandra N, Garrett DS, Gronenborn AM, Bax A, Clore GM (1997) Defining long range order in NMR
structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy. Nat Struct Bioi 4: 443-9.
Tolman JR, Flanagan JM, Kennedy MA, Prestegard JH (1995) Nuclear magnetic dipole interactions in
field-oriented proteins: information for structure determination in solution. Proc Nat! Acad Sci
USA 92: 9279-83.
Ubbink M, Bendall DS (1997). Complex of plastocyanin and cytochrome c characterized by NMR
chemical shift analysis. Biochemistry 36: 6326-6335.
Valcarce C, Selander-Sunnerhagen M, Tamlitz AM, Drakenberg T, Bjork J, Stenflo J (1993) Calcium
affinity of the NH,-terminal epidermal growth factor-like module of factor X. Effect of the gammacarboxyglutamic acid-containing module. J Bioi Chern 268: 26673-26678.
van Heijenoort C, Penin F, Guiltet E (1998) Dynamics of the DNA binding domain of the fructose
repressor from the analysis of linear correlations between the 15N_ 1 H bond spectral densities
obtained by nuclear magnetic resonance spectroscopy. Biochemistry 37: 5060-73.
Wendolski JJ, Mathew JB (1989). Molecular dynamic effects on protein electrostatics. Proteins: Struct
Funct Genet 5: 3l3-32l.
Wishart DS, Sykes BD, Richards FM (1992) The chemical shift index: a fast and simple method for the
assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31: 1647 -5l.
Wishart DS, Sykes BD (1994) The l3C chemical-shift index: a simple method for the identification of
protein secondary structure using 13C chemical-shift data. J Biomol NMR 4: 171-180.
Wishart DS, Bigam CG, Yao J, Abildgaard F, Dyson HJ, Oldfield E, Markley JL, Sykes BD (1995) IH, l3C
and 15N chemical shift referencing in biomolecular NMR. J Biomol NMR 6: l35-140.
Woessner DE (1962) Nuclear spin relaxation in ellipsoids undergoing rotational Brownian motion. J.
Chern. Phys. 3: 647-654.
Wong KB, Daggett V (1998) Barstar has a highly dynamic hydrophobic core: evidence from molecular
dynamics simulations and nuclear magnetic resonance relaxation data. Biochemistry 37: 11182-92.
Yang D, Komat R, Kay LE (1997) A Multidimensional NMR Experiment for Measurement of the Protein Dihedral Angle Based on Cross-Correlated Relaxation between IH_13C Dipolar and 13C' (Carbonyl) Chemical Shift Anisotropy Mechanisms, J Am Chern Soc 119: 11938-11940.
B. BERSCH et al.: Protein Structure and Dynamics by NMR in Solution
Sattler M, Fesik SW (1996) Use of deuterium labeling in NMR: overcoming a sizeable problem. Structure 4: 1245-9.
Shuker SB, Hajduk pJ, Meadows RP, Fesik SW (1996) Discovering high-affinity ligands for proteins:
SAR by NMR. Science 274: 1531-1534.
Spera S, Bax A (1991) Empirical correlation between protein backbone conformation and C a and C~
l3C nuclear magnetic resonance chemical shifts J Am Chern Soc 1l3: 5490-5492.
Thielens NM, Aude CA, Lacroix MB, Gagnon J, Arlaud GJ (1990) Ca ' + binding properties and Ca ' +_
dependent interactions of the isolated N-terminal alpha fragments of human complement proteases C1r and CIs. J Bioi Chern 265, 14469-14475.
Thielens NM, Emie K, Lacroix M, Jaquinod M, Hernandez JF, Esser AF, Arlaud GF (1998) The
N-terminal CUB-EGF module pair of human complement protease C1r binds Ca ' + with high
affinity and mediates Ca'+-dependent interaction with CIs. J Bioi Chern 274: 9149-9159.
Tiede DM, Vashishta AC, Gunner MR (1993) Electron-transfer kinetics and electrostatic properties of
the Rhodobacter sphaeroides reaction center and soluble c cytochromes. Biochemistry 32:
4514-453l.
Tjandra N, Bax A (1997) Direct measurement of distances and angles in biomolecules by NMR in a
dilute liquid crystalline medium. Science 278: 1111- 1114.
Tjandra N, Garrett DS, Gronenborn AM, Bax A, Clore GM (1997) Defining long range order in NMR
structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy. Nat Struct Bioi 4: 443-9.
Tolman JR, Flanagan JM, Kennedy MA, Prestegard JH (1995) Nuclear magnetic dipole interactions in
field-oriented proteins: information for structure determination in solution. Proc Nat! Acad Sci
USA 92: 9279-83.
Ubbink M, Bendall DS (1997). Complex of plastocyanin and cytochrome c characterized by NMR
chemical shift analysis. Biochemistry 36: 6326-6335.
Valcarce C, Selander-Sunnerhagen M, Tamlitz AM, Drakenberg T, Bjork J, Stenflo J (1993) Calcium
affinity of the NH,-terminal epidermal growth factor-like module of factor X. Effect of the gammacarboxyglutamic acid-containing module. J Bioi Chern 268: 26673-26678.
van Heijenoort C, Penin F, Guiltet E (1998) Dynamics of the DNA binding domain of the fructose
repressor from the analysis of linear correlations between the 15N_ 1 H bond spectral densities
obtained by nuclear magnetic resonance spectroscopy. Biochemistry 37: 5060-73.
Wendolski JJ, Mathew JB (1989). Molecular dynamic effects on protein electrostatics. Proteins: Struct
Funct Genet 5: 3l3-32l.
Wishart DS, Sykes BD, Richards FM (1992) The chemical shift index: a fast and simple method for the
assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31: 1647 -5l.
Wishart DS, Sykes BD (1994) The l3C chemical-shift index: a simple method for the identification of
protein secondary structure using 13C chemical-shift data. J Biomol NMR 4: 171-180.
Wishart DS, Bigam CG, Yao J, Abildgaard F, Dyson HJ, Oldfield E, Markley JL, Sykes BD (1995) IH, l3C
and 15N chemical shift referencing in biomolecular NMR. J Biomol NMR 6: l35-140.
Woessner DE (1962) Nuclear spin relaxation in ellipsoids undergoing rotational Brownian motion. J.
Chern. Phys. 3: 647-654.
Wong KB, Daggett V (1998) Barstar has a highly dynamic hydrophobic core: evidence from molecular
dynamics simulations and nuclear magnetic resonance relaxation data. Biochemistry 37: 11182-92.
Yang D, Komat R, Kay LE (1997) A Multidimensional NMR Experiment for Measurement of the Protein Dihedral Angle Based on Cross-Correlated Relaxation between IH_13C Dipolar and 13C' (Carbonyl) Chemical Shift Anisotropy Mechanisms, J Am Chern Soc 119: 11938-11940.