Hydrogen bonding and equilibrium protium-deuterium fractionation factors in the immunoglobulin G binding domain of protein G

被引:24
作者
Khare, D [1 ]
Alexander, P [1 ]
Orban, J [1 ]
机构
[1] Univ Maryland, Maryland Biotechnol Inst, Ctr Adv Res Biotechnol, Rockville, MD 20850 USA
关键词
D O I
10.1021/bi9827114
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protium-deuterium fractionation factors (phi) were determined for more than 85% of the backbone amide protons in the IgG binding domains of protein G, G(B1) and G(B2), from NMR spectra recorded over a range of H2O/D2O solvent ratios. Previous studies suggest a correlation between phi and hydrogen bond strength; amide and hydroxyl groups in strong hydrogen bonds accumulate protium (phi < 1), while weak hydrogen bonds accumulate deuterium (phi > 1). Our results show that the alpha-helical residues have slightly lower phi values (1.03 +/- 0.05) than beta-sheet residues (1.12 +/- 0.07), on average. The lowest phi value obtained (0.65) does not involve a backbone amide but rather is for the interaction between two side chains, Y45 and D47. Fractionation factors for solvent-exposed residues are between the alpha-helix and beta-sheet values, on average, and are close to those for random coil peptides. Further, the difference in phi(av) between alpha-helix and solvent-exposed residues is small, suggesting that differences in hydrogen bond strength for intrachain hydrogen bonds and amide...water hydrogen bonds are also small. Overall, the enrichment for deuterium suggests that most backbone...backbone hydrogen bonds are weak.
引用
收藏
页码:3918 / 3925
页数:8
相关论文
共 47 条
[1]   1.67-ANGSTROM X-RAY STRUCTURE OF THE B2 IMMUNOGLOBULIN-BINDING DOMAIN OF STREPTOCOCCAL PROTEIN-G AND COMPARISON TO THE NMR STRUCTURE OF THE B1 DOMAIN [J].
ACHARI, A ;
HALE, SP ;
HOWARD, AJ ;
CLORE, GM ;
GRONENBORN, AM ;
HARDMAN, KD ;
WHITLOW, M .
BIOCHEMISTRY, 1992, 31 (43) :10449-10457
[2]   THERMODYNAMIC ANALYSIS OF THE FOLDING OF THE STREPTOCOCCAL PROTEIN-G IGG-BINDING DOMAINS B1 AND B2 - WHY SMALL PROTEINS TEND TO HAVE HIGH DENATURATION TEMPERATURES [J].
ALEXANDER, P ;
FAHNESTOCK, S ;
LEE, T ;
ORBAN, J ;
BRYAN, P .
BIOCHEMISTRY, 1992, 31 (14) :3597-3603
[3]   KINETIC-ANALYSIS OF FOLDING AND UNFOLDING THE 56-AMINO ACID IGG-BINDING DOMAIN OF STREPTOCOCCAL PROTEIN-G [J].
ALEXANDER, P ;
ORBAN, J ;
BRYAN, P .
BIOCHEMISTRY, 1992, 31 (32) :7243-7248
[4]   A FAST ALGORITHM FOR RENDERING SPACE-FILLING MOLECULE PICTURES [J].
BACON, D ;
ANDERSON, WF .
JOURNAL OF MOLECULAR GRAPHICS, 1988, 6 (04) :219-220
[5]   HYDROGEN-BONDING IN GLOBULAR-PROTEINS [J].
BAKER, EN ;
HUBBARD, RE .
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, 1984, 44 (02) :97-179
[6]   REMOVAL OF F1-BASE-LINE DISTORTION AND OPTIMIZATION OF FOLDING IN MULTIDIMENSIONAL NMR-SPECTRA [J].
BAX, A ;
IKURA, M ;
KAY, LE ;
ZHU, G .
JOURNAL OF MAGNETIC RESONANCE, 1991, 91 (01) :174-178
[7]   COMPARISON OF DIFFERENT MODES OF 2-DIMENSIONAL REVERSE-CORRELATION NMR FOR THE STUDY OF PROTEINS [J].
BAX, A ;
IKURA, M ;
KAY, LE ;
TORCHIA, DA ;
TSCHUDIN, R .
JOURNAL OF MAGNETIC RESONANCE, 1990, 86 (02) :304-318
[8]   NATURAL ABUNDANCE N-15 NMR BY ENHANCED HETERONUCLEAR SPECTROSCOPY [J].
BODENHAUSEN, G ;
RUBEN, DJ .
CHEMICAL PHYSICS LETTERS, 1980, 69 (01) :185-189
[9]   Hydrogen bonding and equilibrium isotope enrichment in histidine-containing proteins [J].
Bowers, PM ;
Klevit, RE .
NATURE STRUCTURAL BIOLOGY, 1996, 3 (06) :522-531
[10]   LOW-BARRIER HYDROGEN-BONDS AND LOW FRACTIONATION FACTOR BASES IN ENZYMATIC-REACTIONS [J].
CLELAND, WW .
BIOCHEMISTRY, 1992, 31 (02) :317-319