Zobrazeno 1 - 5
of 5
pro vyhledávání: '"S R, Krystek"'
Publikováno v:
Protein science : a publication of the Protein Society. 5(4)
A new functional representation of NMR-derived distance constraints, the flexible restraint potential, has been implemented in the program CONGEN (Bruccoleri RE, Karplus M, 1987, Biopolymers 26:137-168) for molecular structure generation. In addition
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0fc293e45397b6800f2b8d75d5a5c0ce
https://pubmed.ncbi.nlm.nih.gov/8845749
https://pubmed.ncbi.nlm.nih.gov/8845749
Publikováno v:
Protein science : a publication of the Protein Society. 4(1)
Direct comparisons between the recently solved X-ray and NMR structures of human endothelin-1 with respect to secondary structure, RMS deviations, surface accessibilities, and side-chain conformers indicate important differences in conformation, espe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5335369f8f3d694b4b6e6a091ca4801a
https://pubmed.ncbi.nlm.nih.gov/7773179
https://pubmed.ncbi.nlm.nih.gov/7773179
Autor:
S R, Krystek, P S, Patel, P M, Rose, S M, Fisher, B K, Kienzle, D A, Lach, E C, Liu, J S, Lynch, J, Novotny, M L, Webb
Publikováno v:
The Journal of biological chemistry. 269(17)
The molecular basis for endothelin (ET) isopeptide selectivity between ETA and ETB receptors was studied by examining ligand binding to several site-specific mutants of the human ETA receptor. Based on a computer-built three-dimensional model of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b5a3c7870693c6a3e1a864fc5aee1500
https://pubmed.ncbi.nlm.nih.gov/8175640
https://pubmed.ncbi.nlm.nih.gov/8175640
Publikováno v:
Peptide research. 5(3)
Using synthetic peptides, we previously identified portions of the lutropin alpha-subunit that are in contact with the beta-subunit. In order to elucidate structure/function differences of the glycoprotein hormones, a similar study was conducted for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::84d5552b90b1c19b4265b86cd59667d8
https://pubmed.ncbi.nlm.nih.gov/1421805
https://pubmed.ncbi.nlm.nih.gov/1421805
Publikováno v:
Peptide research. 2(4)
We have assessed the hydropathic nature, secondary structure, and flexibility of endothelin and report a testable model for the structure of this 21-amino acid vasoconstrictor peptide. The proposed model consists of a rigid (disulfide bonded), hydrop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::faf060eae1bc289f6266566633cb7d84
https://pubmed.ncbi.nlm.nih.gov/2520767
https://pubmed.ncbi.nlm.nih.gov/2520767