Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Nicholas Panasik"'
Publikováno v:
Europe PubMed Central
4(S)-Hydroxyproline (Hyp) residues constitute about 10% of most forms of collagen, the most abundant protein in vertebrates. X-Ray diffraction analysis was used to ascertain how the structure of proline residues is affected by the inductive effect el
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94cb429b1f750ac01e08f599dcc78005
https://doi.org/10.1111/j.1399-3011.1994.tb00169.x
https://doi.org/10.1111/j.1399-3011.1994.tb00169.x
Autor:
Mohammad Alsayari, Omar Bagasra, Mayank Aggarwal, Naiomi Haynes, Krishna C. Addanki, Samina Noorali, Nicholas Panasik, Kuha Mahalingham
Publikováno v:
The FASEB Journal. 23
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e0550754ee9ee861b645125506002ae6
https://doi.org/10.1096/fasebj.23.1_supplement.361.5
https://doi.org/10.1096/fasebj.23.1_supplement.361.5
Publikováno v:
Biochimica et biophysica acta. 1543(2)
An increasing number of enzymes active at low temperature are being studied to help determine the structural features important for cold-activity. This review examines the diversity of prokaryotic cold-active enzymes and the features proposed to acco
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86a8e6cc86192c560ffb1f00dd67e348
https://pubmed.ncbi.nlm.nih.gov/11150617
https://pubmed.ncbi.nlm.nih.gov/11150617
Publikováno v:
Biochimica et biophysica acta. 1543(1)
Analysis of the structural basis for thermostability in proteins has come mainly from pairwise comparisons of mesophilic and thermophilic structures and has often yielded conflicting results. Interpretation of these results would be enhanced by knowi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95cfa5828c8aeda779f6777af5a9845c
https://pubmed.ncbi.nlm.nih.gov/11087953
https://pubmed.ncbi.nlm.nih.gov/11087953