Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Lesley H, Greene"'
Autor:
Megan A. Hept, Lesley H. Greene
Publikováno v:
MethodsX, Vol 11, Iss , Pp 102341- (2023)
Extraction of high molecular weight (HMW) DNA for long read sequencing with little to no fragmentation and high purity is difficult to acquire from cyanobacterial species. Here we describe a modified method of extraction using Promega's WizardⓇ HMW
Externí odkaz:
https://doaj.org/article/eba2b73a43c94e419383835b8e4e7afc
Publikováno v:
Journal of Computational Chemistry. 42:600-607
Two proteins within the β-grasp superfamily, the B1-domain of protein G and the small archaeal modifier protein 1, were investigated to elucidate the key determinants of structural stability at the level of individual interactions. These symmetrical
Autor:
Lesley H. Greene, Jason P. Agola, James Weifu Lee, Cherrelle L. Barnes, Sana Sherazi, Thu H. Nguyen
Publikováno v:
Gene. 704:49-58
Synthetic biology with genetically engineered (GE) cyanobacteria has the potential to produce valuable products such as biofuels. However, it is also essential to assess the potential risks of synthetic biology technology before it can be widely used
Autor:
Hai Li, Lesley H Greene
Publikováno v:
PLoS ONE, Vol 5, Iss 1, p e8654 (2010)
Chitinases are prevalent in life and are found in species including archaea, bacteria, fungi, plants, and animals. They break down chitin, which is the second most abundant carbohydrate in nature after cellulose. Hence, they are important for maintai
Externí odkaz:
https://doaj.org/article/90e48de2f78d488993405bcb36a01417
Publikováno v:
The protein journal. 38(5)
Understanding and computationally predicting the protein folding process remains one of the most challenging scientific problems and has uniquely garnered the interdisciplinary efforts of researchers from both the biological, chemical, physical and c
Autor:
Cherrelle L. Barnes, Lesley H. Greene, Sana Sherazi, James Weifu Lee, Jason P. Agola, Thu H. Nguyen
Publikováno v:
The FASEB Journal. 33
Publikováno v:
IEEE transactions on nanobioscience. 15(2)
The B1 domain of protein G (GB1) is a small, 56 amino acid bacterial immunoglobulin-binding protein with a 4β+ α fold. Architecturally, it is composed of a two-layer sandwich consisting of a four-stranded β -sheet that packs against an α -helix.
Autor:
Raffaella Ugolini, Lorna J. Smith, Heike I. Rösner, Christina Redfield, Victoria A. Higman, Lesley H. Greene
Publikováno v:
Journal of Biomolecular Nmr
Backbone 15N relaxation parameters and 15N–1HN residual dipolar couplings (RDCs) have been measured for a variant of human α-lactalbumin (α-LA) in 4, 6, 8 and 10 M urea. In the α-LA variant, the eight cysteine residues in the protein have been r
Autor:
Keith Brew, Evangelia D. Chrysina, K.R. Acharya, L.I. Irons, Lesley H. Greene, Anastassios C. Papageorgiou
Publikováno v:
Protein Science. 10:2301-2316
Serum retinol binding protein (RBP) is a member of the lipocalin family, proteins with up-and-down beta-barrel folds, low levels of sequence identity, and diverse functions. Although tryptophan 24 of RBP is highly conserved among lipocalins, it does
Autor:
Richard Charles Garratt, Alison L. Cuff, Lesley H. Greene, Annabel E. Todd, Ian Sillitoe, Christine A. Orengo, Oliver C. Redfern, Tony Lewis, Mark Dibley, Janet M. Thornton, Adam J. Reid, Timothy J. Dallman, Frances M. G. Pearl
Publikováno v:
Structure(London, England:1993)
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
This paper explores the structural continuum in CATH and the extent to which superfamilies adopt distinct folds. Although most superfamilies are structurally conserved, in some of the most highly populated superfamilies (4% of all superfamilies) ther