Related ArticlesHeteronuclear 2D NMR studies of an engineered insulin monomer: assignment and characterization of the receptor-binding surface by selective 2H and 13C labeling with application to protein design.
Biochemistry. 1991 Jul 30;30(30):7373-89
Authors: Weiss MA, Hua QX, Lynch CS, Frank BH, Shoelson SE
Insulin provides an important model for the application of genetic engineering to rational protein design and has been well characterized in the crystal state. However, self-association of insulin in solution has precluded complementary 2D NMR study under physiological conditions. We demonstrate here that such limitations may be circumvented by the use of a monomeric analogue that contains three amino acid substitutions on the protein surface (HisB10----Asp, ProB28----Lys, and LysB29----Pro); this analogue (designated DKP-insulin) retains native receptor-binding potency. Comparative 1H NMR studies of native human insulin and a series of three related analogues--(i) the singly substituted analogue [HisB10----Asp], (ii) the doubly substituted analogue [ProB28----Lys; LysB29----Pro], and (iii) DKP-insulin--demonstrate progressive reduction in concentration-dependent line-broadening in accord with the results of analytical ultracentrifugation. Extensive nonlocal interactions are observed in the NOESY spectrum of DKP-insulin, indicating that this analogue adopts a compact and stably folded structure as a monomer in overall accord with crystal models. Site-specific 2H and 13C isotopic labels are introduced by semisynthesis as probes for the structure and dynamics of the receptor-binding surface. These studies confirm and extend under physiological conditions the results of a previous 2D NMR analysis of native insulin in 20% acetic acid [Hua, Q. X., & Weiss, M. A. (1991) Biochemistry 30, 5505-5515]. Implications for the role of protein flexibility in receptor recognition are discussed with application to the design of novel insulin analogues.
Solution NMR Studies of A? Monomer Dynamics.
Solution NMR Studies of A? Monomer Dynamics.
Solution NMR Studies of A? Monomer Dynamics.
Protein Pept Lett. 2011 Jan 11;
Authors: Wang C
A? is widely recognized as a key molecule in Alzheimer's disease, causing neurotoxicity through A? aggregates such as A? oligomers and fibrils. A?40 and A?42, composed of 40 and 42 residues, respectively, are the major A? species in human brain. A?42 aggregates much faster than A?40 but the mechanism of such difference in aggregation propensity is poorly understood. Using NMR spin relaxation, we have shown that...
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[NMR paper] Complete assignment of heteronuclear protein resonances by protonless NMR spectroscop
Complete assignment of heteronuclear protein resonances by protonless NMR spectroscopy.
Related Articles Complete assignment of heteronuclear protein resonances by protonless NMR spectroscopy.
Angew Chem Int Ed Engl. 2005 May 13;44(20):3089-92
Authors: Bermel W, Bertini I, Duma L, Felli IC, Emsley L, Pierattelli R, Vasos PR
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[NMR paper] NMR spectroscopic studies of the DNA-binding domain of the monomer-binding nuclear or
NMR spectroscopic studies of the DNA-binding domain of the monomer-binding nuclear orphan receptor, human estrogen related receptor-2. The carboxyl-terminal extension to the zinc-finger region is unstructured in the free form of the protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles NMR spectroscopic studies of the DNA-binding domain of the monomer-binding nuclear orphan receptor, human estrogen related receptor-2. The carboxyl-terminal extension to the zinc-finger region...
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[NMR paper] Automated resonance assignment of proteins using heteronuclear 3D NMR. 2. Side chain
Automated resonance assignment of proteins using heteronuclear 3D NMR. 2. Side chain and sequence-specific assignment.
Related Articles Automated resonance assignment of proteins using heteronuclear 3D NMR. 2. Side chain and sequence-specific assignment.
J Chem Inf Comput Sci. 1997 May-Jun;37(3):467-77
Authors: Li KB, Sanctuary BC
A sequential assignment protocol for proteins was developed using heteronuclear 3D NMR. The protocol consists of an amino acid type recognition algorithm and a primary sequence mapping algorithm. The former measures...
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[NMR paper] Structure and dynamics of a protein assembly. 1H-NMR studies of the 36 kDa R6 insulin
Structure and dynamics of a protein assembly. 1H-NMR studies of the 36 kDa R6 insulin hexamer.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structure and dynamics of a protein assembly. 1H-NMR studies of the 36 kDa R6 insulin hexamer.
J Mol Biol. 1996 Apr 26;258(1):136-57
Authors: Jacoby E, Hua QX, Stern AS, Frank BH, Weiss MA
The structure and dynamics of the R6 human insulin hexamer are investigated by two- and three-dimensional homonuclear 1H-NMR spectroscopy....
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[NMR paper] 1H-NMR assignment and secondary structure of human insulin-like growth factor-I (IGF-
1H-NMR assignment and secondary structure of human insulin-like growth factor-I (IGF-I) in solution.
Related Articles 1H-NMR assignment and secondary structure of human insulin-like growth factor-I (IGF-I) in solution.
J Biochem. 1992 Apr;111(4):529-36
Authors: Sato A, Nishimura S, Ohkubo T, Kyogoku Y, Koyama S, Kobayashi M, Yasuda T, Kobayashi Y
Human insulin-like growth factor-I (IGF-I) was studied by two-dimensional 1H-NMR spectroscopy. Resonance assignments were obtained for all the backbone protons and almost all of the sidechain protons...
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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] Heteronuclear 2D NMR studies of an engineered insulin monomer: assignment and charact
Heteronuclear 2D NMR studies of an engineered insulin monomer: assignment and characterization of the receptor-binding surface by selective 2H and 13C labeling with application to protein design.
Related Articles Heteronuclear 2D NMR studies of an engineered insulin monomer: assignment and characterization of the receptor-binding surface by selective 2H and 13C labeling with application to protein design.
Biochemistry. 1991 Jul 30;30(30):7373-89
Authors: Weiss MA, Hua QX, Lynch CS, Frank BH, Shoelson SE
Insulin provides an important model for...
Heteronuclear 2D NMR studies of an engineered insulin monomer: assignment and charact
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