Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Courtney B. Taylor"'
Autor:
Courtney B. Taylor, Gregg T. Beckham, Clare McCabe, Michael E. Himmel, Christina M. Payne, Michael F. Crowley
Publikováno v:
The Journal of Physical Chemistry B. 117:4924-4933
In nature, processive and non-processive cellulase enzymes deconstruct cellulose to soluble sugars. From structural studies, the consensus is that processive cellulases exhibit tunnels lined with aromatic and polar residues, whereas non-processive ce
Publikováno v:
Journal of Applied Research in Intellectual Disabilities. 25:383-391
Background Although participation in faith communities is important to many individuals with disabilities, few studies have examined differences between communities that are more (versus less) inclusive. This study investigated characteristics of fai
Autor:
Malin Bergenstråhle, Courtney B. Taylor, Xiongce Zhao, John W. Brady, Yannick J. Bomble, Lintao Bu, James F. Matthews, John M. Yarbrough, Jakob Wohlert, Gregg T. Beckham, Stephen R. Decker, William S. Adney, Clare McCabe, Michael F. Crowley, Michael E. Himmel, Michael G. Resch
Publikováno v:
Biophysical Journal. 99(11):3773-3781
Fungi and bacteria secrete glycoprotein cocktails to deconstruct cellulose. Cellulose-degrading enzymes (cellulases) are often modular, with catalytic domains for cellulose hydrolysis and carbohydrate-binding modules connected by linkers rich in seri
Autor:
M. Faiz Talib, William S. Adney, Lintao Bu, Michael E. Himmel, Clare McCabe, Gregg T. Beckham, Courtney B. Taylor, Michael F. Crowley
Carbohydrate-binding modules (CBMs) are ubiquitous components of glycoside hydrolases, which degrade polysaccharides in nature. CBMs target specific polysaccharides, and CBM binding affinity to cellulose is known to be proportional to cellulase activ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d099a4bad06eddfba76549abd54ff9b8
https://europepmc.org/articles/PMC3270969/
https://europepmc.org/articles/PMC3270969/
Autor:
Michael F. Crowley, Courtney B. Taylor, Gregg T. Beckham, Yannick J. Bomble, Michael E. Himmel, Christina M. Payne, Clare McCabe
Publikováno v:
The Journal of biological chemistry. 286(47)
Proteins employ aromatic residues for carbohydrate binding in a wide range of biological functions. Glycoside hydrolases, which are ubiquitous in nature, typically exhibit tunnels, clefts, or pockets lined with aromatic residues for processing carboh