15N NMR relaxation studies of calcium-loaded parvalbumin show tight dynamics compared to those of other EF-hand proteins
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15N NMR relaxation studies of calcium-loaded parvalbumin show tight dynamics compared to those of other EF-hand proteins. / Baldellon, C; Alattia, J R; Strub, M P; Pauls, T; Berchtold, M W; Cavé, A; Padilla, A.
In: Biochemistry, Vol. 37, No. 28, 1998, p. 9964-75.Research output: Contribution to journal › Journal article › Research › peer-review
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T1 - 15N NMR relaxation studies of calcium-loaded parvalbumin show tight dynamics compared to those of other EF-hand proteins
AU - Baldellon, C
AU - Alattia, J R
AU - Strub, M P
AU - Pauls, T
AU - Berchtold, M W
AU - Cavé, A
AU - Padilla, A
N1 - Keywords: Amides; Animals; Calcium-Binding Proteins; Models, Molecular; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Parvalbumins; Protein Conformation; Protein Structure, Secondary; Protons; Rats; Thermodynamics
PY - 1998
Y1 - 1998
N2 - Dynamics of the rat alpha-parvalbumin calcium-loaded form have been determined by measurement of 15N nuclear relaxation using proton-detected heteronuclear NMR spectroscopy. The relaxation data were analyzed using spectral density functions and the Lipari-Szabo formalism. The major dynamic features for the rat alpha-parvalbumin calcium-loaded form are (1) the extreme rigidity of the helix-loop-helix EF-hand motifs and the linker segment connecting them, (2) the N and C termini of the protein being restricted in their mobility, (3) a conformational exchange occurring at the kink of helix D, and (4) the residue at relative position 2 in the Ca2+-binding sites having an enhanced mobility. Comparison of the Ca2+-binding EF-hand domains of alpha-parvalbumin-Ca2+, calbindin-Ca2+, and calmodulin-Ca2+ shows that parvalbumin is probably the most rigid of the EF-hand proteins. It also illustrates the dynamical properties which are conserved in the EF-hand domains from different members of this superfamily: (1) a tendency toward higher mobility of NH vectors at relative position 2 in the Ca2+-binding loop, (2) a restricted mobility for the other residues in the binding loop, and (3) an overall rigidity for the helices of EF-hand motifs. The differences in mobility between parvalbumin and the two EF-hand proteins occur mainly at the linker connecting the pair of EF hands and also at the C terminus of the last helix. In parvalbumin-Ca2+, these two regions are characterized by a pronounced rigidity compared to the corresponding more mobile regions in calbindin-Ca2+ and calmodulin-Ca2+.
AB - Dynamics of the rat alpha-parvalbumin calcium-loaded form have been determined by measurement of 15N nuclear relaxation using proton-detected heteronuclear NMR spectroscopy. The relaxation data were analyzed using spectral density functions and the Lipari-Szabo formalism. The major dynamic features for the rat alpha-parvalbumin calcium-loaded form are (1) the extreme rigidity of the helix-loop-helix EF-hand motifs and the linker segment connecting them, (2) the N and C termini of the protein being restricted in their mobility, (3) a conformational exchange occurring at the kink of helix D, and (4) the residue at relative position 2 in the Ca2+-binding sites having an enhanced mobility. Comparison of the Ca2+-binding EF-hand domains of alpha-parvalbumin-Ca2+, calbindin-Ca2+, and calmodulin-Ca2+ shows that parvalbumin is probably the most rigid of the EF-hand proteins. It also illustrates the dynamical properties which are conserved in the EF-hand domains from different members of this superfamily: (1) a tendency toward higher mobility of NH vectors at relative position 2 in the Ca2+-binding loop, (2) a restricted mobility for the other residues in the binding loop, and (3) an overall rigidity for the helices of EF-hand motifs. The differences in mobility between parvalbumin and the two EF-hand proteins occur mainly at the linker connecting the pair of EF hands and also at the C terminus of the last helix. In parvalbumin-Ca2+, these two regions are characterized by a pronounced rigidity compared to the corresponding more mobile regions in calbindin-Ca2+ and calmodulin-Ca2+.
U2 - 10.1021/bi980334p
DO - 10.1021/bi980334p
M3 - Journal article
C2 - 9665701
VL - 37
SP - 9964
EP - 9975
JO - Biochemistry
JF - Biochemistry
SN - 0006-2960
IS - 28
ER -
ID: 11175475