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Original

Structural modulation of calmodulin and calmodulin-dependent protein kinase II by pea protein hydrolysates

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Pages 178-189 | Published online: 06 Jul 2009

References

  • Barnette MS, Daly R, Weiss B. Inhibition of calmodulin activity by insect venom peptides. Biochem Pharmacol 1983; 32: 2929–2933
  • Burger D, Cox JA, Comte M, Stein EA. Sequential conformational changes in calmodulin upon binding of calcium. Biochemistry 1984; 23: 1966–1971
  • Chin D, Means AR. Calmodulin: a prototypical calcium sensor. Trends Cell Biol 2000; 10: 322–328
  • Chin D, Means AR. Mechanisms for regulation of calmodulin kinase IIα by Ca2 + /calmodulin and autophosphorylation of threonine 286. Biochemistry 2002; 41: 14001–14009
  • Cho MJ, Vaghy PL, Kondo R, Lee SH, Davis JP, Rehl R, Heo WD, Johnson JD. Reciprocal regulation of mammalian nitric oxide synthase and calcineurin by plant calmodulin isoforms. Biochemistry 1998; 37: 15593–15597
  • Dedman JR, Potter JD, Jackson RL, Johnson JD, Means AR. Physicochemical properties of rat testis Ca2 + -dependent regulator protein of cyclic nucleotide phosphodiesterase. Relationship of Ca2 + -binding, conformational changes, and phosphodiesterase activity. J Biol Chem 1977; 252: 8415–8422
  • Fan MZ, Sauer WC, Jaikaran S. Amino acid and energy digestibility in peas (Pisum sativum) from white-flowered spring cultivars for growing pigs. J Sci Food Agric 1994; 64: 249–256
  • Gangopadhyay JP, Grabarek Z, Ikemoto N. Fluorescence probe study of Ca2 + -dependent interactions of calmodulin with calmodulin-binding peptides of the ryanodine receptor. Biochem Biophys Res Commun 2004; 323: 760–768
  • Harmat V, Bocskei Z, Naray-Szabo G, Bata I, Csutor AS, Hermecz I, Aranyi P, Szabo B, Liliom K, Vertessy BG, Ovadi J. A new potent calmodulin antagonist with arylalkylamine structure: crystallographic, spectroscopic and functional studies. J Mol Biol 2000; 297: 747–755
  • Hennesey JP, Parthasarathy M, Johnson WC. Conformational transitions of calmodulin as studied by vacuum-UV CD. Biopolymers 1987; 26: 561–571
  • Hook SS, Means AR. Ca2 + /CaM-dependent kinases: from activation to function. Ann Rev Pharmacol Toxicol 2001; 41: 471–505
  • Itano T, Itano R, Penniston JT. Interactions of basic polypeptides and proteins with calmodulin. Biochem J 1980; 189: 455–459
  • Kilhoffer MC, Demaille JG, Gérard D. Tyrosine fluorescence of ram testis and octopus calmodulins. Effects of calcium, magnesium, and ionic strength. Biochemistry 1981; 20: 4407–4414
  • Kizawa K. Calmodulin binding peptide comprising α-casein exorphin sequence. J Agric Food Chem 1997; 45: 1579–1581
  • Kizawa K, Naganuma K, Murakami U. Calmodulin-binding peptides isolated from α-casein peptone. J Dairy Res 1995; 62: 587–592
  • Kuboniwa H, Tjandra N, Grzesiek S, Ren H, Klee CB, Bax A. Solution structure of calcium-free calmodulin. Nat Struct Biol 1995; 2: 768–776
  • LaPorte DC, Wierman BM, Storm DR. Calcium-induced exposure of a hydrophobic surface on calmodulin. Biochemistry 1980; 19: 3814–3819
  • Li H, Aluko RE. Kinetics of the inhibition of calcium/calmodulin-dependent protein kinase II by pea protein-derived peptides. J Nutr Bioch 2005; 16: 656–662
  • Malenick DA, Anderson SR. Binding of simple peptides, hormones, and neurotransmitters by calmodulin. Biochemistry 1982; 21: 3480–3486
  • Maune JF, Beckingham K, Martin SR, Bayley PM. Circular dichroism studies on calcium binding to two series of Ca2 +  binding site mutants of Drosophila melanogaster calmodulin. Biochemistry 1992; 31: 7779–7786
  • Persechini A, Kretsinger RH. The central helix of calmodulin functions as a flexible tether. J Biol Chem 1988; 263: 12175–12178
  • Pinto APA, Campana PT, Beltramini LM, Silber AM, Araujo APU. Structural characterization of a recombinant flagellar calcium-binding protein from Trypanosoma cruzi. Biochim Biophys Acta 2003; 1652: 107–114
  • Qin Y, Liu J, Li X, Wei Q. Preparation and characterization of a single-chain calcineurin-calmodulin complex. Biochim Biophys Acta 2005; 1652: 171–178
  • Roberts PR, Burney JD, Black KW, Zaloga GP. Effect of chain length on absorption of biologically active peptides from the gastrointestinal tract. Digestion 1999; 60: 332–337
  • Rodger A, Ismail MA. Introduction to circular dichroism. Spectrophotometry and spectrofluorimetry, MG Gore. Oxford University Press, New York 2000; 99–139
  • Schmid FX. Spectra methods of characterizing protein conformation and conformational changes. Protein structure: a practical approach, TE Creighton. Oxford University Press, New York 1990; 251–285
  • Strickland EH. Aromatic contributions to circular dichroism spectra of proteins. CRC Crit Rev Biochem 1974; 2: 113–175
  • Stryer L. The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. J Mol Biol 1965; 13: 482–495
  • Yang C, Jas GS, Kuczera K. Structure, dynamics and interaction with kinase targets: computer simulations of calmodulin. Biochim Biophys Acta 2004; 1697: 289–300
  • Zhang M, Tanaka T, Ikura M. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nat Struct Biol 1995; 2: 758–767

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