[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...
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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...
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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...
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[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...
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[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...
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[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...
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08-22-2010 03:03 PM
[NMR paper] Loop mobility in a four-helix-bundle protein: 15N NMR relaxation measurements on huma
Loop mobility in a four-helix-bundle protein: 15N NMR relaxation measurements on human interleukin-4.
Related Articles Loop 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...
Deletion of the N- or C-Terminal Helix of ApolipophorinIII To Create a Four-Helix Bundle Protein
Linear Mode
