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231223s2004 xx ||||| 00| ||eng c |
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|a pubmed24n0482.xml
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|a (DE-627)NLM144513862
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|a (NLM)14745807
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Yao, Xiao L
|e verfasserin
|4 aut
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| 245 |
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|a Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR
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|c 2004
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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| 338 |
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|a Band
|b nc
|2 rdacarrier
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| 500 |
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|a Date Completed 22.03.2005
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|a Date Revised 21.11.2013
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|a published: Print
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|a Citation Status MEDLINE
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| 520 |
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|a Copyright 2004 John Wiley & Sons, Ltd.
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|a Elastin is the main structural protein that provides elasticity to various tissues and organs in vertebrates. Molecular motions are believed to play a significant role in its elasticity. We have used solid-state NMR spectroscopy to characterize the dynamics of an elastin-mimetic protein as a function of hydration to better understand the origin of elastin elasticity. Poly(Lys-25), [(VPGVG)(4)(VPGKG)](39), has a repeat sequence common to natural elastin. (13)C cross-polarization and direct polarization spectra at various hydration levels indicate that water enhances the protein motion in a non-uniform manner. Below 20% hydration, the backbone motion increases only slightly whereas above 30% hydration, both the backbone and the side-chains undergo large-amplitude motions. The motional amplitudes are extracted from (13)C-(1)H and (1)H-(1)H dipolar couplings using 2D isotropic-anisotropic correlation experiments. The root mean square fluctuation angles are found to be 11-18 degrees in the dry protein and 16-21 degrees in the 20% hydrated protein. Dramatically, the amplitudes increase to near isotropic at 30% hydration. Field-dependent (1)H rotating-frame spin-lattice relaxation times (T(1rho)) indicate that significant motions occur on the microsecond time-scale (1.2-2.3 micros). The large-amplitude and low-frequency motion of poly(Lys-25) at relatively mild hydration indicates that the conformational entropy of the protein in the relaxed state contributes significantly to the elasticity
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Research Support, U.S. Gov't, Non-P.H.S.
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| 650 |
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|a Carbon Isotopes
|2 NLM
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| 650 |
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|a Peptide Fragments
|2 NLM
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| 650 |
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|a Peptides
|2 NLM
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|a Polylysine
|2 NLM
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| 650 |
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|a 25104-18-1
|2 NLM
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| 650 |
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|a Hydrogen
|2 NLM
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| 650 |
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7 |
|a 7YNJ3PO35Z
|2 NLM
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| 650 |
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7 |
|a Elastin
|2 NLM
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| 650 |
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|a 9007-58-3
|2 NLM
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| 700 |
1 |
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|a Conticello, Vincent P
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Hong, Mei
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Magnetic resonance in chemistry : MRC
|d 1985
|g 42(2004), 2 vom: 15. Feb., Seite 267-75
|w (DE-627)NLM098179667
|x 1097-458X
|7 nnns
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| 773 |
1 |
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|g volume:42
|g year:2004
|g number:2
|g day:15
|g month:02
|g pages:267-75
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|a AR
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|d 42
|j 2004
|e 2
|b 15
|c 02
|h 267-75
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