Related ArticlesLoop mobility in a four-helix-bundle protein: 15N NMR relaxation measurements on human interleukin-4.
Biochemistry. 1992 Nov 3;31(43):10431-7
Authors: Redfield C, Boyd J, Smith LJ, Smith RA, Dobson CM
15N NOE, T1, and T2 measurements have been carried out on uniformly 15N-labeled human interleukin-4. Analysis of the results in terms of order parameters (S2) shows that although the helical core of this four-helix-bundle protein exists as a well-defined structure with limited conformational flexibility (S2 congruent to 0.9), other regions of the molecule experience substantial fluctuations in the conformation of the main chain (S2 = 0.3-0.8). These regions include both the N- and C-termini and two of the loops joining the helices. The majority of these internal motions are fast compared with the overall rotational correlation time (tau R = 7.6 ns at 35 degrees C) and are localized in regions that are relatively ill-defined in the NMR structures previously determined for this protein [Smith, L. J., Redfield, C., Boyd, J., Lawrence, G. M. P., Edwards, R. G., Smith, R. A. G., & Dobson, C. M. (1992) J. Mol. Biol. 224, 899-904]. Other motions are on a slower time scale and appear to be associated with two of the three disulfide bonds and the beta-sheet region in the protein. The dynamic properties of interleukin-4 in solution have been compared with features of the X-ray structures of other four-helix-bundle proteins. The results suggest that the dynamic properties observed here may be general for this class of proteins and may be significant for the interpretation of both their structural and functional properties.
Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Angew Chem Int Ed Engl. 2011 Mar 18;
Authors: Salmon L, Ortega Roldan JL, Lescop E, Licinio A, van Nuland N, Jensen MR, Blackledge M
nmrlearner
Journal club
0
03-23-2011 05:41 PM
[NMR paper] Thermodynamic interpretation of protein dynamics from NMR relaxation measurements.
Thermodynamic interpretation of protein dynamics from NMR relaxation measurements.
Related Articles Thermodynamic interpretation of protein dynamics from NMR relaxation measurements.
Protein Pept Lett. 2005 Apr;12(3):235-40
Authors: Spyracopoulos L
Protein dynamics and thermodynamics can be characterized through measurements of relaxation rates of side chain (2)H and (13)C, and backbone (15)N nuclei using NMR spectroscopy. The rates reflect protein motions on timescales from picoseconds to milliseconds. Backbone and methyl side chain NMR...
nmrlearner
Journal club
0
11-25-2010 08:21 PM
[NMR paper] Redesign of a four-helix bundle protein by phage display coupled with proteolysis and
Redesign of a four-helix bundle protein by phage display coupled with proteolysis and structural characterization by NMR and X-ray crystallography.
Related Articles Redesign of a four-helix bundle protein by phage display coupled with proteolysis and structural characterization by NMR and X-ray crystallography.
J Mol Biol. 2002 Oct 18;323(2):253-62
Authors: Chu R, Takei J, Knowlton JR, Andrykovitch M, Pei W, Kajava AV, Steinbach PJ, Ji X, Bai Y
To test whether it is practical to use phage display coupled with proteolysis for protein design, we...
nmrlearner
Journal club
0
11-24-2010 08:58 PM
[NMR paper] Solid-state NMR data support a helix-loop-helix structural model for the N-terminal h
Solid-state NMR data support a helix-loop-helix structural model for the N-terminal half of HIV-1 Rev in fibrillar form.
Related Articles Solid-state NMR data support a helix-loop-helix structural model for the N-terminal half of HIV-1 Rev in fibrillar form.
J Mol Biol. 2001 Nov 2;313(4):845-59
Authors: Blanco FJ, Hess S, Pannell LK, Rizzo NW, Tycko R
Rev is a 116 residue basic protein encoded by the genome of human immunodeficiency virus type 1 (HIV-1) that binds to multiple sites in the Rev response element (RRE) of viral mRNA transcripts in...
nmrlearner
Journal club
0
11-19-2010 08:44 PM
[NMR paper] Dynamics of a de novo designed three-helix bundle protein studied by 15N, 13C, and 2H
Dynamics of a de novo designed three-helix bundle protein studied by 15N, 13C, and 2H NMR relaxation methods.
Related Articles Dynamics of a de novo designed three-helix bundle protein studied by 15N, 13C, and 2H NMR relaxation methods.
Biochemistry. 2001 Aug 14;40(32):9560-9
Authors: Walsh ST, Lee AL, DeGrado WF, Wand AJ
Understanding how the amino acid sequence of a polypeptide chain specifies a unique, functional three-dimensional structure remains an important goal, especially in the context of the emerging discipline of de novo protein...
nmrlearner
Journal club
0
11-19-2010 08:44 PM
[NMR paper] NMR structure of the hRap1 Myb motif reveals a canonical three-helix bundle lacking t
NMR structure of the hRap1 Myb motif reveals a canonical three-helix bundle lacking the positive surface charge typical of Myb DNA-binding domains.
Related Articles NMR structure of the hRap1 Myb motif reveals a canonical three-helix bundle lacking the positive surface charge typical of Myb DNA-binding domains.
J Mol Biol. 2001 Sep 7;312(1):167-75
Authors: Hanaoka S, Nagadoi A, Yoshimura S, Aimoto S, Li B, de Lange T, Nishimura Y
Mammalian telomeres are composed of long tandem arrays of double-stranded telomeric TTAGGG repeats associated with...
nmrlearner
Journal club
0
11-19-2010 08:44 PM
[NMR paper] Leptin is a four-helix bundle: secondary structure by NMR.
Leptin is a four-helix bundle: secondary structure by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Leptin is a four-helix bundle: secondary structure by NMR.
FEBS Lett. 1997 Apr 28;407(2):239-42
Authors: Kline AD, Becker GW, Churgay LM, Landen BE, Martin DK, Muth WL, Rathnachalam R, Richardson JM, Schoner B, Ulmer M, Hale JE
Leptin is a signaling protein that in its mutant forms has been associated with obesity and Type II diabetes. The lack of sequence...
nmrlearner
Journal club
0
08-22-2010 03:31 PM
[NMR paper] Leptin is a four-helix bundle: secondary structure by NMR.
Leptin is a four-helix bundle: secondary structure by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Leptin is a four-helix bundle: secondary structure by NMR.
FEBS Lett. 1997 Apr 28;407(2):239-42
Authors: Kline AD, Becker GW, Churgay LM, Landen BE, Martin DK, Muth WL, Rathnachalam R, Richardson JM, Schoner B, Ulmer M, Hale JE
Leptin is a signaling protein that in its mutant forms has been associated with obesity and Type II diabetes. The lack of sequence...
Loop mobility in a four-helix-bundle protein: 15N NMR relaxation measurements on huma
Linear Mode
