Solution structure and dynamics of bovine b -lactoglobulin A

: Using heteronuclear NMR spectroscopy, we studied the solution structure and dynamics of bovine b -lactoglobulin A at pH 2.0 and 45 8 C, where the protein exists as a monomeric native state. The monomeric NMR structure, comprising an eight-stranded continuous antiparallel b -barrel and one major a -helix, is similar to the X-ray dimeric structure obtained at pH 6.2, including b I strand that forms the dimer interface and loop EF that serves as a lid of the interior hydrophobic hole. $ 1 H % - 15 N NOE revealed that b F , b G , and b H strands buried under the major a -helix are rigid on a pico- to nanosecond time scale and also emphasized rapid fluctuations of loops and the N- and C-terminal regions.

[1]  J Collinge,et al.  Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations. , 1999, Science.

[2]  B. Qin,et al.  12‐Bromododecanoic acid binds inside the calyx of bovine β‐lactoglobulin , 1998 .

[3]  H. Molinari,et al.  Monomeric bovine β‐lactoglobulin adopts a β‐barrel fold at pH 2 , 1998 .

[4]  E N Baker,et al.  Structural basis of the Tanford transition of bovine beta-lactoglobulin. , 1998, Biochemistry.

[5]  D. Uhrín,et al.  Complete assignment of 1H, 13C and 15N chemical shifts for bovine β-lactoglobulin: Secondary structure and topology of the native state is retained in a partially unfolded form , 1998, Journal of biomolecular NMR.

[6]  K. Wüthrich,et al.  Torsion angle dynamics for NMR structure calculation with the new program DYANA. , 1997, Journal of molecular biology.

[7]  S. Prusiner,et al.  Prion diseases and the BSE crisis. , 1997, Science.

[8]  H. Molinari,et al.  Identification of a conserved hydrophobic cluster in partially folded bovine beta-lactoglobulin at pH 2. , 1997, Folding & design.

[9]  Darren R. Flower,et al.  Bovine β-lactoglobulin at 1.8 Å resolution — still an enigmatic lipocalin , 1997 .

[10]  Christopher M. Dobson,et al.  Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis , 1997, Nature.

[11]  S. Balasubramanian,et al.  Transmuting a helices and b sheets , 1997 .

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

[13]  T. Tanaka,et al.  High helical propensity of the peptide fragments derived from beta-lactoglobulin, a predominantly beta-sheet protein. , 1995, Journal of molecular biology.

[14]  K. Nishikawa,et al.  Trifluoroethanol-induced Stabilization of the α-Helical Structure of β-Lactoglobulin: Implication for Non-hierarchical Protein Folding , 1995 .

[15]  T. Pawson,et al.  Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation. , 1994, Biochemistry.

[16]  L. Kay,et al.  A gradient 13C NOESY-HSQC experiment for recording NOESY spectra of 13C-labeled proteins dissolved in H2O , 1993 .

[17]  Robert Powers,et al.  Relationships between the precision of high-resolution protein NMR structures, solution-order parameters, and crystallographic B factors , 1993 .

[18]  E. Goldsmith,et al.  Structural basis of latency in plasminogen activator inhibitor-1 , 1992, Nature.

[19]  L. Kay,et al.  Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1 beta. , 1989, Biochemistry.

[20]  R. Doolittle,et al.  A simple method for displaying the hydropathic character of a protein. , 1982, Journal of molecular biology.