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Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences.
Chem Rev. 2006 May;106(5):1624-71. doi: 10.1021/cr040421p.
Chem Rev. 2006.
PMID: 16683748
Review.
No abstract available.
Comparison of the backbone dynamics of a natural and a consensus designed 3-TPR domain.
Jarymowycz VA, Cortajarena AL, Regan L, Stone MJ.
Jarymowycz VA, et al.
J Biomol NMR. 2008 Jul;41(3):169-78. doi: 10.1007/s10858-008-9250-6. Epub 2008 Jun 20.
J Biomol NMR. 2008.
PMID: 18566891
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Comparison between the backbone dynamics of an 11-amino acid peptide sequence in alpha-helical and beta-hairpin structural contexts.
Jarymowycz VA, Krupinska E, Stone MJ.
Jarymowycz VA, et al.
Biochemistry. 2006 Sep 19;45(37):11179-89. doi: 10.1021/bi0608919.
Biochemistry. 2006.
PMID: 16964979
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Repeat motions and backbone flexibility in designed proteins with different numbers of identical consensus tetratricopeptide repeats.
Cheng CY, Jarymowycz VA, Cortajarena AL, Regan L, Stone MJ.
Cheng CY, et al. Among authors: jarymowycz va.
Biochemistry. 2006 Oct 3;45(39):12175-83. doi: 10.1021/bi060819a.
Biochemistry. 2006.
PMID: 17002317
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Remote changes in the dynamics of the phosphotyrosine-binding domain of insulin receptor substrate-1 induced by phosphopeptide binding.
Jarymowycz VA, Stone MJ.
Jarymowycz VA, et al.
Biochemistry. 2008 Dec 16;47(50):13371-82. doi: 10.1021/bi801096b.
Biochemistry. 2008.
PMID: 19053277
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