Zobrazeno 1 - 10
of 15
pro vyhledávání: '"N C, Kaarsholm"'
Publikováno v:
Biochemistry. 32:12160-12166
The pro region of carboxypeptidase Y (CPY) from yeast is necessary for the correct folding of the enzyme [Winther, J. R., & Sorensen P. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 9330-9334]. Using fluorescence, circular dichroism, and heteronuclear NMR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c339652cf13323a0252feb01a6d3a92
https://doi.org/10.1021/bi00096a028
https://doi.org/10.1021/bi00096a028
Publikováno v:
Journal of molecular biology. 284(2)
Studies of naturally occuring and chemically modified insulins have established that the NH2-terminal helix of the A-chain is important in conferring affinity in insulin-receptor interactions. Nevertheless, the three-dimensional structural basis for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d45ff70e09c2418b1a55c256dda8cfc6
https://pubmed.ncbi.nlm.nih.gov/9813131
https://pubmed.ncbi.nlm.nih.gov/9813131
Publikováno v:
Journal of molecular biology. 279(1)
Despite years of effort to clarify the structural basis of insulin receptor binding no clear consensus has emerged. It is generally believed that insulin receptor binding is accompanied by some degree of conformational change in the carboxy-terminal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::360cfca9316143b229ed1eb01017e96d
https://pubmed.ncbi.nlm.nih.gov/9636695
https://pubmed.ncbi.nlm.nih.gov/9636695
Publikováno v:
The Journal of biological chemistry. 272(2)
Magnetic circular dichroism (MCD) spectra of a series of adducts formed by the Co(II)-substituted R-state insulin hexamer are reported. The His-B10 residues in this hexamer form tris imidazole chelates in which pseudotetrahedral Co(II) centers are co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::cabed0c4419ff0151670e34511ec6c90
https://pubmed.ncbi.nlm.nih.gov/8995407
https://pubmed.ncbi.nlm.nih.gov/8995407
Publikováno v:
Proteins. 26(4)
The insulin hexamer is an allosteric protein exhibiting both positive and negative cooperative homotropic interactions and positive cooperative heterotropic interactions (C. R. Bloom et al., J. Mol. Biol. 245, 324-330, 1995). In this study, detailed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d9b4bec746c73b1a269926636cf4ecbf
https://pubmed.ncbi.nlm.nih.gov/8990494
https://pubmed.ncbi.nlm.nih.gov/8990494
Publikováno v:
Biochemistry. 35(27)
Insulin circulates in the bloodstream and binds to its specific cell-surface receptor as a 5808 Da monomeric species. However, studies of the monomer structure and dynamics in solution are severely limited by insulin self-association into dimers and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ca6b5b10d6b689e36fd3a48740c3ee59
https://pubmed.ncbi.nlm.nih.gov/8688419
https://pubmed.ncbi.nlm.nih.gov/8688419
Publikováno v:
Peptides 1994 ISBN: 9789072199218
Peptides 1994
Peptides 1994
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cd796aeb841a2bb90b5a50a031066e59
https://doi.org/10.1007/978-94-011-1468-4_405
https://doi.org/10.1007/978-94-011-1468-4_405
Autor:
N C, Kaarsholm, S, Ludvigsen
Publikováno v:
Receptor. 5(1)
Studies of naturally occurring and chemically modified insulins indicate that relatively few of the 51 amino acid residues may be assigned specific roles in insulin-receptor interactions. Most of the insulin X-ray structural information is derived fr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::87d5fd0e1187cbc591b2ee9cb665d39b
https://pubmed.ncbi.nlm.nih.gov/7613479
https://pubmed.ncbi.nlm.nih.gov/7613479
Publikováno v:
Advances in experimental medicine and biology. 338
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::dafada040d8b2f649a004bd6888bf10f
https://pubmed.ncbi.nlm.nih.gov/8304222
https://pubmed.ncbi.nlm.nih.gov/8304222
Publikováno v:
The Journal of biological chemistry. 267(13)
One- and two-dimensional 1H NMR spectroscopy have been employed to probe the association and subsequent conformational changes of metal-free insulin in sodium chloride solution at pH 9 and 9.4. These studies establish that the proton resonances of Hi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0056c0d15280a22118a37734226afc20
https://pubmed.ncbi.nlm.nih.gov/1577733
https://pubmed.ncbi.nlm.nih.gov/1577733