{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,9,16]],"date-time":"2024-09-16T19:51:02Z","timestamp":1726516262294},"reference-count":63,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2003,1,1]],"date-time":"2003-01-01T00:00:00Z","timestamp":1041379200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,8,17]],"date-time":"2013-08-17T00:00:00Z","timestamp":1376697600000},"content-version":"vor","delay-in-days":3881,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biophysical Journal"],"published-print":{"date-parts":[[2003,1]]},"DOI":"10.1016\/s0006-3495(03)74834-6","type":"journal-article","created":{"date-parts":[[2009,1,6]],"date-time":"2009-01-06T12:33:32Z","timestamp":1231245212000},"page":"82-101","source":"Crossref","is-referenced-by-count":2,"title":["Structural Preference for Changes in the Direction of the Ca2+-Induced Transition: A Study of the Regulatory Domain of Skeletal Troponin-C"],"prefix":"10.1016","volume":"84","author":[{"given":"Felicia","family":"Pitici","sequence":"first","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/S0006-3495(03)74834-6_bib1","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1002\/prot.340170408","article-title":"Essential dynamics of proteins","volume":"17","author":"Amadei","year":"1993","journal-title":"Proteins"},{"key":"10.1016\/S0006-3495(03)74834-6_bib2","doi-asserted-by":"crossref","first-page":"2733","DOI":"10.1103\/PhysRevLett.80.2733","article-title":"Vibrational dynamics of folded proteins: significance of slow and fast motions in relationship to function","volume":"80","author":"Bahar","year":"1998","journal-title":"Phys. Rev. Lett."},{"key":"10.1016\/S0006-3495(03)74834-6_bib3","doi-asserted-by":"crossref","first-page":"2567","DOI":"10.1021\/jp9536920","article-title":"Principal component analysis and long time protein dynamics","volume":"100","author":"Balsera","year":"1996","journal-title":"J. Phys. Chem."},{"key":"10.1016\/S0006-3495(03)74834-6_bib4","unstructured":"Biosym Technologies 1998. InsightII, version 97.2."},{"key":"10.1016\/S0006-3495(03)74834-6_bib5","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1002\/jcc.540040211","article-title":"CHARMM: A program for macromolecular energy, minimization, and dynamics calculations","volume":"4","author":"Brooks","year":"1983","journal-title":"J. Comp. Chem."},{"key":"10.1016\/S0006-3495(03)74834-6_bib6","doi-asserted-by":"crossref","first-page":"4995","DOI":"10.1073\/pnas.82.15.4995","article-title":"Normal modes for specific motions of macromolecules: Application to the hinge-bending mode of lysozyme","volume":"82","author":"Brooks","year":"1985","journal-title":"Proc. Natl. Acad. Sci. USA"},{"year":"1988","series-title":"A theoretical perspective of dynamics, structure, and thermodynamics","author":"Brooks","key":"10.1016\/S0006-3495(03)74834-6_bib7"},{"key":"10.1016\/S0006-3495(03)74834-6_bib8","doi-asserted-by":"crossref","first-page":"1522","DOI":"10.1002\/jcc.540161209","article-title":"Harmonic analysis of large systems. I Methodology","volume":"16","author":"Brooks","year":"1995","journal-title":"J. Comp. Chem."},{"key":"10.1016\/S0006-3495(03)74834-6_bib9","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/0022-2836(92)90136-8","article-title":"A 500ps molecular dynamics simulation study of interleukin-1\u03b2 in water","volume":"226","author":"Chandrasekhar","year":"1992","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0006-3495(03)74834-6_bib10","doi-asserted-by":"crossref","first-page":"3288","DOI":"10.1073\/pnas.92.8.3288","article-title":"A sampling problem in molecular dynamics simulations of macromolecules","volume":"92","author":"Clarage","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0006-3495(03)74834-6_bib11","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1038\/scientificamerican1175-36","article-title":"The protein switch of muscle contraction","volume":"233","author":"Cohen","year":"1975","journal-title":"Sci. Am."},{"key":"10.1016\/S0006-3495(03)74834-6_bib12","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1016\/S0006-3495(95)80203-1","article-title":"Molecular dynamics simulations of the glucocorticoid receptor DNA-binding domain in complex with DNA and free in solution","volume":"68","author":"Eriksson","year":"1995","journal-title":"Biophys. J."},{"key":"10.1016\/S0006-3495(03)74834-6_bib13","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1006\/jmbi.1999.2770","article-title":"Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations","volume":"289","author":"Evenas","year":"1999","journal-title":"J. Mol. Biol."},{"year":"1985","series-title":"Enzyme structure and mechanism","author":"Fersht","key":"10.1016\/S0006-3495(03)74834-6_bib14"},{"key":"10.1016\/S0006-3495(03)74834-6_bib15","doi-asserted-by":"crossref","first-page":"784","DOI":"10.1038\/nsb0995-784","article-title":"Structures of the troponin C regulatory domains in the apo and calcium-saturated states","volume":"2","author":"Gagne","year":"1995","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/S0006-3495(03)74834-6_bib16","doi-asserted-by":"crossref","first-page":"4386","DOI":"10.1021\/bi963076+","article-title":"Mechanism of direct coupling between binding and induced structural change in regulatory calcium binding proteins","volume":"36","author":"Gagne","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/S0006-3495(03)74834-6_bib17","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1006\/jmbi.1998.1723","article-title":"Backbone and methyl dynamics of the regulatory domain of troponin C: anisotropic rotational diffusion and contribution of conformational entropy to calcium affinity","volume":"278","author":"Gagne","year":"1998","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0006-3495(03)74834-6_bib18","doi-asserted-by":"crossref","first-page":"6633","DOI":"10.1021\/bi00241a001","article-title":"On the role of methionine residues in the sequence-independent recognition of nonpolar protein surfaces","volume":"30","author":"Gellman","year":"1991","journal-title":"Biochemistry"},{"key":"10.1016\/S0006-3495(03)74834-6_bib19","first-page":"13121","article-title":"Proteolytic fragments of troponin C","volume":"256","author":"Grabareck","year":"1981","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0006-3495(03)74834-6_bib20","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1038\/345132a0","article-title":"Inhibition of mutant troponin C activity by an intradomian disulfide bond","volume":"345","author":"Grabarek","year":"1990","journal-title":"Nature"},{"key":"10.1016\/S0006-3495(03)74834-6_bib21","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1002\/(SICI)1097-0134(199703)27:3<425::AID-PROT10>3.0.CO;2-N","article-title":"Model-free methods of analyzing domain motions in proteins from simulation: a comparison of normal mode analysis and molecular dynamics simulation of lysozyme","volume":"27","author":"Hayward","year":"1997","journal-title":"Proteins"},{"key":"10.1016\/S0006-3495(03)74834-6_bib22","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1016\/0022-2836(88)90208-2","article-title":"Refined crystal structure of troponin C from turkey skeletal muscle at 2.0\u00c5 resolution","volume":"203","author":"Herzberg","year":"1988","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0006-3495(03)74834-6_bib23","doi-asserted-by":"crossref","first-page":"1695","DOI":"10.1016\/S0969-2126(97)00315-8","article-title":"Structures of four Ca2+-bound troponin C at 2.0\u00c5 resolution: further insights into the Ca2+-switch in the calmodulin superfamily","volume":"5","author":"Houdusse","year":"1997","journal-title":"Structure"},{"key":"10.1016\/S0006-3495(03)74834-6_bib24","doi-asserted-by":"crossref","first-page":"1543","DOI":"10.1002\/jcc.540161210","article-title":"Harmonic analysis of large systems. II Comparison of different protein models","volume":"16","author":"Janezic","year":"1995","journal-title":"J. Comp. Chem."},{"key":"10.1016\/S0006-3495(03)74834-6_bib25","doi-asserted-by":"crossref","first-page":"1554","DOI":"10.1002\/jcc.540161211","article-title":"Harmonic analysis of large systems. III Comparison with molecular dynamics","volume":"16","author":"Janezic","year":"1995","journal-title":"J. Comp. Chem."},{"key":"10.1016\/S0006-3495(03)74834-6_bib26","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1063\/1.445869","article-title":"Comparison of simple potential functions for simualting liquid water","volume":"79","author":"Jorgensen","year":"1983","journal-title":"J. Chem. Phys."},{"key":"10.1016\/S0006-3495(03)74834-6_bib27","doi-asserted-by":"crossref","first-page":"922","DOI":"10.1107\/S0567739476001873","article-title":"A solution for the best rotation to relate two sets of vectors","volume":"32","author":"Kabsch","year":"1976","journal-title":"Acta Crystallogr. A"},{"key":"10.1016\/S0006-3495(03)74834-6_bib28","doi-asserted-by":"crossref","first-page":"119","DOI":"10.3109\/10409238009105467","article-title":"Structure and evolution of calcium-modulated proteins","volume":"8","author":"Kretsinger","year":"1980","journal-title":"CRC Crit. Rev. Biochem."},{"key":"10.1016\/S0006-3495(03)74834-6_bib29","doi-asserted-by":"crossref","first-page":"235","DOI":"10.3109\/10409238409108717","article-title":"Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction","volume":"16","author":"Leavis","year":"1984","journal-title":"CRC Crit. Rev. Biochem."},{"key":"10.1016\/S0006-3495(03)74834-6_bib30","doi-asserted-by":"crossref","first-page":"8330","DOI":"10.1021\/bi00026a014","article-title":"Calcium binding to the regulatory N-domain of skeletal muscle troponin C occurs in a stepwise manner","volume":"34","author":"Li","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/S0006-3495(03)74834-6_bib31","doi-asserted-by":"crossref","first-page":"12519","DOI":"10.1021\/bi971222l","article-title":"NMR studies of Ca2+ binding to the regulatory domains of cardiac and E41A skeletal muscle troponin C reveal the importance of site I to energetics of the induced structural changes","volume":"36","author":"Li","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/S0006-3495(03)74834-6_bib32","doi-asserted-by":"crossref","first-page":"1721","DOI":"10.1002\/bip.360240906","article-title":"Structural analysis of carboxypeptidase A and its complexes with inhibitors as a basis for modeling enzyme recognition and specificity","volume":"24","author":"Liebman","year":"1985","journal-title":"Biopolymers"},{"key":"10.1016\/S0006-3495(03)74834-6_bib33","doi-asserted-by":"crossref","first-page":"4546","DOI":"10.1021\/ja00381a009","article-title":"Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules","volume":"104","author":"Lipari","year":"1982","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/S0006-3495(03)74834-6_bib34","doi-asserted-by":"crossref","first-page":"3586","DOI":"10.1021\/jp973084f","article-title":"All-atom empirical potential for molecular modeling and dynamics studies of proteins","volume":"102","author":"MacKerell","year":"1998","journal-title":"J. Phys. Chem. B"},{"year":"1991","series-title":"Dynamics of proteins and nucleic acids","author":"McCammon","key":"10.1016\/S0006-3495(03)74834-6_bib35"},{"key":"10.1016\/S0006-3495(03)74834-6_bib36","doi-asserted-by":"crossref","first-page":"28494","DOI":"10.1074\/jbc.272.45.28494","article-title":"Interaction of the second binding region of troponin I with the regulatory domain of skeletal muscle troponin C as determined by NMR spectroscopy","volume":"272","author":"McKay","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0006-3495(03)74834-6_bib37","doi-asserted-by":"crossref","first-page":"12419","DOI":"10.1021\/bi9809019","article-title":"Structure and interaction site of the regulatory domain of troponin-C when complexed with the 96\u2013148 region of troponin-I","volume":"37","author":"McKay","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/S0006-3495(03)74834-6_bib38","doi-asserted-by":"crossref","first-page":"1718","DOI":"10.1126\/science.8259515","article-title":"Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures","volume":"262","author":"Meador","year":"1993","journal-title":"Science"},{"key":"10.1016\/S0006-3495(03)74834-6_bib39","doi-asserted-by":"crossref","first-page":"11284","DOI":"10.1074\/jbc.271.19.11284","article-title":"The role of Phe-92 in the Ca2+-induced conformational transition in the C-terminal domain of calmodulin","volume":"271","author":"Meyer","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0006-3495(03)74834-6_bib40","doi-asserted-by":"crossref","first-page":"812","DOI":"10.1002\/(SICI)1096-987X(19970430)18:6<812::AID-JCC6>3.0.CO;2-V","article-title":"Optimal position of the solute for simulations","volume":"18","author":"Mezei","year":"1997","journal-title":"J. Comp. Chem."},{"key":"10.1016\/S0006-3495(03)74834-6_bib41","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1126\/science.8310294","article-title":"Diverse essential functions revealed by complementing yeast calmodulin mutants","volume":"263","author":"Ohya","year":"1994","journal-title":"Science"},{"key":"10.1016\/S0006-3495(03)74834-6_bib42","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1002\/pro.5560070206","article-title":"An interaction-based analysis of Ca2+-sensor proteins","volume":"7","author":"Nelson","year":"1998","journal-title":"Protein Sci."},{"key":"10.1016\/S0006-3495(03)74834-6_bib43","doi-asserted-by":"crossref","first-page":"794","DOI":"10.1002\/pro.5560060406","article-title":"Intermolecular tuning of calmodulin by target peptides and proteins: differential effects on Ca2+ binding and implications for kinase activation","volume":"6","author":"Peersen","year":"1997","journal-title":"Protein Sci."},{"key":"10.1016\/S0006-3495(03)74834-6_bib44","unstructured":"Pitici, F. 1999. Structural and dynamic determinants for calcium-dependent properties of troponin-C and calmodulin: a computational study. Ph.D. thesis. Mount Sinai School of Medicine of NYU, New York. 105 pp."},{"key":"10.1016\/S0006-3495(03)74834-6_bib45","first-page":"397a","article-title":"Ca2+-sensing mechanisms in calmodulin and troponin-C","volume":"80","author":"Pitici","year":"2001","journal-title":"Biophys. J."},{"key":"10.1016\/S0006-3495(03)74834-6_bib46","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1093\/protein\/7.1.109","article-title":"A calmodulin-target peptide hybrid molecule with unique calcium-binding properties","volume":"7","author":"Porumb","year":"1994","journal-title":"Protein Eng."},{"key":"10.1016\/S0006-3495(03)74834-6_bib47","series-title":"Calcium in Muscle Activation: A Comparative Approach","first-page":"44","author":"Ruegg","year":"1986"},{"key":"10.1016\/S0006-3495(03)74834-6_bib48","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/0021-9991(77)90098-5","article-title":"Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes","volume":"23","author":"Ryckaert","year":"1977","journal-title":"J. Comp. Phys."},{"key":"10.1016\/S0006-3495(03)74834-6_bib49","unstructured":"Sali, A., R. Sanchez, and A. Badretdinov. 1997. MODELLER - a program for protein structure modeling, version 4."},{"key":"10.1016\/S0006-3495(03)74834-6_bib50","doi-asserted-by":"crossref","first-page":"15953","DOI":"10.1021\/bi00049a010","article-title":"NMR solution structure of calcium-saturated skeletal muscle troponin C","volume":"34","author":"Slupsky","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/S0006-3495(03)74834-6_bib51","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1006\/jmbi.1997.1257","article-title":"Structural details of a calcium induced molecular switch: x-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.7\u00c5 resolution","volume":"273","author":"Strynadka","year":"1997","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0006-3495(03)74834-6_bib52","doi-asserted-by":"crossref","first-page":"4843","DOI":"10.1073\/pnas.79.16.4843","article-title":"Electronic distributions within protein phenylalanine aromatic rings are reflected by the three-dimensional oxygen atom environments","volume":"79","author":"Thomas","year":"1982","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0006-3495(03)74834-6_bib53","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1006\/jmbi.1993.1135","article-title":"Normal mode analysis of G-actin","volume":"230","author":"Tirion","year":"1993","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0006-3495(03)74834-6_bib54","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1002\/prot.340220107","article-title":"The essential dynamics of thermolysin: confirmation of the hinge-bending motion and comparison of simulations in vacuum and water","volume":"22","author":"van Aalten","year":"1995","journal-title":"Proteins"},{"key":"10.1016\/S0006-3495(03)74834-6_bib55","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1093\/protein\/8.11.1129","article-title":"Essential dynamics of the cellular retinol-binding protein - evidence for ligand-induced conformational changes","volume":"8","author":"van Aalten","year":"1995","journal-title":"Protein Eng."},{"key":"10.1016\/S0006-3495(03)74834-6_bib56","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1007\/BF01076558","article-title":"Protein engineering and NMR studies of calmodulin","volume":"149","author":"Vogel","year":"1995","journal-title":"Mol. Cell. Biochem."},{"key":"10.1016\/S0006-3495(03)74834-6_bib57","doi-asserted-by":"crossref","first-page":"11102","DOI":"10.1021\/ja972139o","article-title":"Rational design of a calcium sensing system based on induced conformational changes of calmodulin","volume":"119","author":"Vukasinovic","year":"1997","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/S0006-3495(03)74834-6_bib58","doi-asserted-by":"crossref","first-page":"5109","DOI":"10.1021\/bi9600153","article-title":"Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides","volume":"35","author":"Wimley","year":"1996","journal-title":"Biochemistry"},{"year":"1975","series-title":"Thermal vibrations in crystallography","author":"Willis","key":"10.1016\/S0006-3495(03)74834-6_bib59"},{"key":"10.1016\/S0006-3495(03)74834-6_bib60","doi-asserted-by":"crossref","first-page":"1622","DOI":"10.1016\/S0006-3495(98)77876-2","article-title":"Structure and dynamics of calmodulin in solution","volume":"74","author":"Wriggers","year":"1998","journal-title":"Biophys. J."},{"key":"10.1016\/S0006-3495(03)74834-6_bib61","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/S0167-4838(99)00043-6","article-title":"Effects of high pressure and temperature on the wild-type and F29W mutant forms of the N-domain of avian troponin-C","volume":"1431","author":"Yu","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/S0006-3495(03)74834-6_bib62","doi-asserted-by":"crossref","first-page":"15546","DOI":"10.1016\/S0021-9258(17)40714-9","article-title":"The effect of Met\u2192Leu mutations on calmodulin\u2019s ability to activate cyclic nucletide phosphodiesterase","volume":"269","author":"Zhang","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0006-3495(03)74834-6_bib63","doi-asserted-by":"crossref","first-page":"7678","DOI":"10.1016\/S0021-9258(18)34434-X","article-title":"A structural role for the Ca2+-Mg2+ sites on troponin C in the regulation of muscle contraction. Preparation and properties of troponin C depleted myofibrils","volume":"257","author":"Zot","year":"1982","journal-title":"J. Biol. Chem."}],"container-title":["Biophysical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349503748346?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349503748346?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,9,29]],"date-time":"2021-09-29T11:20:18Z","timestamp":1632914418000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006349503748346"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2003,1]]},"references-count":63,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2003,1]]}},"alternative-id":["S0006349503748346"],"URL":"https:\/\/doi.org\/10.1016\/s0006-3495(03)74834-6","relation":{},"ISSN":["0006-3495"],"issn-type":[{"type":"print","value":"0006-3495"}],"subject":[],"published":{"date-parts":[[2003,1]]}}}