[NMR paper] Relating side-chain mobility in proteins to rotameric transitions: insights from mole
Relating side-chain mobility in proteins to rotameric transitions: insights from molecular dynamics simulations and NMR.
Related Articles Relating side-chain mobility in proteins to rotameric transitions: insights from molecular dynamics simulations and NMR.
J Biomol NMR. 2005 Jun;32(2):151-62
Authors: Hu H, Hermans J, Lee AL
The dynamic aspect of proteins is fundamental to understanding protein stability and function. One of the goals of NMR studies of side-chain dynamics in proteins is to relate spin relaxation rates to discrete...
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[NMR paper] Metal-dependent conformational changes in a recombinant vWF-A domain from human facto
Metal-dependent conformational changes in a recombinant vWF-A domain from human factor B: a solution study by circular dichroism, fourier transform infrared and (1)H NMR spectroscopy.
Related Articles Metal-dependent conformational changes in a recombinant vWF-A domain from human factor B: a solution study by circular dichroism, fourier transform infrared and (1)H NMR spectroscopy.
J Mol Biol. 2000 Apr 21;298(1):135-47
Authors: Hinshelwood J, Perkins SJ
Factor B is a key component of the alternative pathway of complement and is cleaved by...
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[NMR paper] Internal mobility of reactive-site-hydrolyzed recombinant Cucurbita maxima trypsin in
Internal mobility of reactive-site-hydrolyzed recombinant Cucurbita maxima trypsin inhibitor-V characterized by NMR spectroscopy: evidence for differential stabilization of newly formed C- and N-termini.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Internal mobility of reactive-site-hydrolyzed recombinant Cucurbita maxima trypsin inhibitor-V characterized by NMR spectroscopy: evidence for differential stabilization of newly formed C- and N-termini.
Biochemistry. 1996 Sep 24;35(38):12503-10
...
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[NMR paper] Solution structure of the B-chain of insulin as determined by 1H NMR spectroscopy. Co
Solution structure of the B-chain of insulin as determined by 1H NMR spectroscopy. Comparison with the crystal structure of the insulin hexamer and with the solution structure of the insulin monomer.
Related Articles Solution structure of the B-chain of insulin as determined by 1H NMR spectroscopy. Comparison with the crystal structure of the insulin hexamer and with the solution structure of the insulin monomer.
Int J Pept Protein Res. 1995 Nov;46(5):424-33
Authors: Hawkins B, Cross K, Craik D
The solution structure of the isolated B-chain of...
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[NMR paper] Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: sequential
Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: sequential resonance assignment and implications for protein dynamics and receptor recognition.
Related Articles Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: sequential resonance assignment and implications for protein dynamics and receptor recognition.
Biochemistry. 1991 Jun 4;30(22):5505-15
Authors: Hua QX, Weiss MA
The solution structure and dynamics of human insulin are investigated by 2D 1H NMR spectroscopy in reference to a previously...
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[NMR paper] Conformational studies on a peptide fragment representing the RNA-binding N-terminus
Conformational studies on a peptide fragment representing the RNA-binding N-terminus of a viral coat protein using circular dichroism and NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Conformational studies on a peptide fragment representing the RNA-binding N-terminus of a viral coat protein using circular dichroism and NMR spectroscopy.
Eur J Biochem. 1991 Oct 15;201(2):489-94
Authors: van der Graaf M, Hemminga MA
...
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[NMR paper] Conformational studies on a peptide fragment representing the RNA-binding N-terminus
Conformational studies on a peptide fragment representing the RNA-binding N-terminus of a viral coat protein using circular dichroism and NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Conformational studies on a peptide fragment representing the RNA-binding N-terminus of a viral coat protein using circular dichroism and NMR spectroscopy.
Eur J Biochem. 1991 Oct 15;201(2):489-94
Authors: van der Graaf M, Hemminga MA
...
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[NMR paper] Solution structure of the carboxyl terminus of a human class Mu glutathione S-transfe
Solution structure of the carboxyl terminus of a human class Mu glutathione S-transferase: NMR assignment strategies in large proteins.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solution structure of the carboxyl terminus of a human class Mu glutathione S-transferase: NMR assignment strategies in large proteins.
J Mol Biol. 1999 Feb 5;285(5):2119-32
Authors: McCallum SA, Hitchens TK, Rule GS
Strategies to obtain the NMR assignments for the HN, N, CO, Calpha and...
Recombinant A22Gâ??B31R-human insulin. A22 addition introduces conformational mobility in B chain C-terminus
Linear Mode
