Zobrazeno 1 - 10
of 17
pro vyhledávání: '"R W, Woody"'
Autor:
Marcia S. Pottle, David J. Evans, Sydney J. Leach, R. W. Woody, George Némethy, E. R. Stimson, J. R. McQuie, S. Lee, Elizabeth Minasian, Samuel Krimm, J. Bandekar, Harold A. Scheraga
Publikováno v:
International Journal of Peptide and Protein Research. 19:187-205
Conformational energy calculations indicate that the peptide backbones of the low-energy conformations of the cyclized dipeptide derivatives cyclo (L-alanyl-L-alanyl-epsilon-aminocaproyl) and cyclo (L-alanyl-D-alanyl-epsilon-aminocaproyl) are constra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e2c34863e1f5b927fcb9dbb629477773
https://doi.org/10.1111/j.1399-3011.1982.tb02608.x
https://doi.org/10.1111/j.1399-3011.1982.tb02608.x
Autor:
R. W. Woody, S.S. Zimmerman, Harold A. Scheraga, John A. Smith, Zachary I. Hodes, Sydney J. Leach, J.A. Weigold, Ian D. Rae, George Némethy, Elizabeth Minasian
Publikováno v:
International Journal of Peptide and Protein Research. 17:575-592
The conformational properties of the N-acetyl-N'-methylamides of the dipeptides lysyl-lysine, lysyl-tyrosine, tyrosyl-lysine, and tyrosyl-tyrosine were studied by means of conformational energy calculations, by n.m.r. measurements in deuterated dimet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89d15dab091d8f9cdb8302e0f3f9dc75
https://doi.org/10.1111/j.1399-3011.1981.tb02031.x
https://doi.org/10.1111/j.1399-3011.1981.tb02031.x
Molecular Dynamics Simulations of Carbonmonoxy Myoglobin and Calculations of Heme Circular Dichroism
Publikováno v:
Insulin & Related Proteins-Structure to Function and Pharmacology ISBN: 9781402006555
The Soret circular dichroism (CD) spectrum of carbonmonoxy myoglobin differs strikingly for the two heme isomers: Δe421=+90 M 1cm 1 for isomer A, Δe421=−7 M 1cm 1 A, for isomer B (Aojula et al., 1988). This observation implies significant differe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f4be423c708dc98bed88058b6feb6e98
https://doi.org/10.1007/0-306-47582-0_18
https://doi.org/10.1007/0-306-47582-0_18
Autor:
P, Hensley, M L, Doyle, D G, Myszka, R W, Woody, M R, Brigham-Burke, C L, Erickson-Miller, C A, Griffin, C S, Jones, D E, McNulty, S P, O'Brien, B Y, Amegadzie, L, MacKenzie, M D, Ryan, P R, Young
Publikováno v:
Methods in enzymology. 323
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::94f6b0543e18069b6f5a60f10e92a904
https://pubmed.ncbi.nlm.nih.gov/10944753
https://pubmed.ncbi.nlm.nih.gov/10944753
Autor:
N, Sreerama, R W, Woody
Publikováno v:
Proteins. 36(4)
A significant fraction of the so-called "random coil" residues in globular proteins exists in the left-handed poly(Pro)II conformation. In order to compare the behavior of this secondary structure with that of the other regular secondary structures,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6fb0358076c97baa99f9411c20abfa36
https://pubmed.ncbi.nlm.nih.gov/10450081
https://pubmed.ncbi.nlm.nih.gov/10450081
Publikováno v:
Chirality. 9(5-6)
By use of an asymmetric Ullmann coupling involving chiral naphthalene oxazolines 1, the title compounds were prepared in good yields and with high diastereoselectivity. Hydrolysis of the binaphthyl oxazolines 2 led to the di-aldehydes 5, which were t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bd22f654ae12036c905738fc5181c804
https://pubmed.ncbi.nlm.nih.gov/9329175
https://pubmed.ncbi.nlm.nih.gov/9329175
Publikováno v:
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme. 41(1)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b8bf6fb96ca0f866c051c9be3fe8ebd2
https://pubmed.ncbi.nlm.nih.gov/8584742
https://pubmed.ncbi.nlm.nih.gov/8584742
Autor:
N, Sreerama, R W, Woody
Publikováno v:
Journal of molecular biology. 242(4)
Different approaches to improve the analysis of protein secondary structure from circular dichroism spectra are compared. Grouping proteins based on the similarity of their circular dichroism spectra, using cluster analysis methods, was utilized as a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6d41fa587710e7fcc805339c9dec93da
https://pubmed.ncbi.nlm.nih.gov/7932706
https://pubmed.ncbi.nlm.nih.gov/7932706
Publikováno v:
Journal of molecular biology. 237(1)
It has been demonstrated that the amino acids Asp537, Asp812, Lys631, His811 and Tyr639 are involved in bacteriophage T7 RNA polymerase catalysis. In the present paper, we report kinetic, spectroscopic and calorimetric characterization of the wild-ty
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::960e19a1d4b71ed0d3c7c8b4eab5f244
https://pubmed.ncbi.nlm.nih.gov/8133519
https://pubmed.ncbi.nlm.nih.gov/8133519
Publikováno v:
Annual Review of Physical Chemistry. 20:407-448
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a1442576acd419b3414262873351ee1e
https://doi.org/10.1146/annurev.pc.20.100169.002203
https://doi.org/10.1146/annurev.pc.20.100169.002203