Daragan VA - Search Results

1

Lactose binding to human galectin-7 (p53-induced gene 1) induces long-range effects through the protein resulting in increased dimer stability and evidence for positive cooperativity.

Ermakova E, Miller MC, Nesmelova IV, López-Merino L, Berbís MA, Nesmelov Y, Tkachev YV, Lagartera L, Daragan VA, André S, Cañada FJ, Jiménez-Barbero J, Solís D, Gabius HJ, Mayo KH. Ermakova E, et al. Among authors: daragan va. Glycobiology. 2013 May;23(5):508-23. doi: 10.1093/glycob/cwt005. Epub 2013 Jan 31. Glycobiology. 2013. PMID: 23376190 Free PMC article.

2

Lactose binding to galectin-1 modulates structural dynamics, increases conformational entropy, and occurs with apparent negative cooperativity.

Nesmelova IV, Ermakova E, Daragan VA, Pang M, Menéndez M, Lagartera L, Solís D, Baum LG, Mayo KH. Nesmelova IV, et al. Among authors: daragan va. J Mol Biol. 2010 Apr 16;397(5):1209-30. doi: 10.1016/j.jmb.2010.02.033. Epub 2010 Feb 23. J Mol Biol. 2010. PMID: 20184898

3

Pro4 prolyl peptide bond isomerization in human galectin-7 modulates the monomer-dimer equilibrum to affect function.

Miller MC, Nesmelova IV, Daragan VA, Ippel H, Michalak M, Dregni A, Kaltner H, Kopitz J, Gabius HJ, Mayo KH. Miller MC, et al. Among authors: daragan va. Biochem J. 2020 Sep 18;477(17):3147-3165. doi: 10.1042/BCJ20200499. Biochem J. 2020. PMID: 32766716 Free PMC article.

4

Heat capacities and a snapshot of the energy landscape in protein GB1 from the pre-denaturation temperature dependence of backbone NH nanosecond fluctuations.

Idiyatullin D, Nesmelova I, Daragan VA, Mayo KH. Idiyatullin D, et al. Among authors: daragan va. J Mol Biol. 2003 Jan 3;325(1):149-62. doi: 10.1016/s0022-2836(02)01155-5. J Mol Biol. 2003. PMID: 12473458

5

Tri- and diglycine backbone rotational dynamics investigated by 13C NMR multiplet relaxation and molecular dynamics simulations.

Daragan VA, Mayo KH. Daragan VA, et al. Biochemistry. 1993 Nov 2;32(43):11488-99. doi: 10.1021/bi00094a004. Biochemistry. 1993. PMID: 8218215

6

Comparison of (13)C(alpha)H and (15)NH backbone dynamics in protein GB1.

Idiyatullin D, Nesmelova I, Daragan VA, Mayo KH. Idiyatullin D, et al. Among authors: daragan va. Protein Sci. 2003 May;12(5):914-22. doi: 10.1110/ps.0228703. Protein Sci. 2003. PMID: 12717014 Free PMC article.

7

Lysine side-chain dynamics derived from 13C-multiplet NMR relaxation studies on di- and tripeptides.

Mikhailov D, Daragan VA, Mayo KH. Mikhailov D, et al. Among authors: daragan va. J Biomol NMR. 1995 Jun;5(4):397-410. doi: 10.1007/BF00182283. J Biomol NMR. 1995. PMID: 7647558

8

13C multiplet nuclear magnetic resonance relaxation-derived ring puckering and backbone dynamics in proline-containing glycine-based peptides.

Mikhailov D, Daragan VA, Mayo KH. Mikhailov D, et al. Among authors: daragan va. Biophys J. 1995 Apr;68(4):1540-50. doi: 10.1016/S0006-3495(95)80326-7. Biophys J. 1995. PMID: 7787039 Free PMC article.

9

A simple approach to analyzing protein side-chain dynamics from 13C NMR relaxation data.

Daragan VA, Mayo KH. Daragan VA, et al. J Magn Reson. 1998 Feb;130(2):329-34. doi: 10.1006/jmre.1997.1310. J Magn Reson. 1998. PMID: 9500896

10

Peptide internal motions on nanosecond time scale derived from direct fitting of (13)C and (15)N NMR spectral density functions.

Mayo KH, Daragan VA, Idiyatullin D, Nesmelova I. Mayo KH, et al. Among authors: daragan va. J Magn Reson. 2000 Sep;146(1):188-95. doi: 10.1006/jmre.2000.2148. J Magn Reson. 2000. PMID: 10968972

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