Search results
Results from the WOW.Com Content Network
Ribbon schematic of Triosephosphate isomerase, hand-drawn by Jane Richardson All-atom contact dots for two well-packed Ala residues. Jane Shelby Richardson (born January 25, 1941) [1] [2] is an American biophysicist best known for developing the Richardson diagram, or ribbon diagram, a method of representing the 3D structure of proteins. [3]
The first 29 amino acids of GHRH were discovered to be as equally potent as its full 44 amino acid structure [1] [2] This fragment became known as GRF (1-29).However, due to a rapid metabolic clearance analogues of GRF (1-29) were synthesized to enhance the biological activity and reduce the rapidity of metabolic clearance.
The Boston Collective work together to teach courses and create books that provide knowledge from women not only in Boston, but women across the nation. These women use their skills and knowledge to provide many women with knowledge about their lives through rhetoric that avoids describing the female reproductive system as passive, unproductive ...
A close analog of a stapled peptide drug invented in the Verdine Lab, sulanemadlin (ALRN-6924), is a first-in-class dual MDM2/MDMX inhibitor currently in Phase II clinical development by Aileron Therapeutics, [4] which he co-founded in 2005. FogPharma, founded in 2016, aims to further develop stapled peptide technology for therapeutic use.
While the timeline primarily focuses on women involved with natural sciences such as astronomy, biology, chemistry and physics, it also includes women from the social sciences (e.g. sociology, psychology) and the formal sciences (e.g. mathematics, computer science), as well as notable science educators and medical scientists. The chronological ...
First Edition, with dust cover. Modern Woman: The Lost Sex is a 1947 work of scientific literature written by Ferdinand Lundberg and Marynia F. Farnham, M.D. which discusses the sociological and psychological context of American women in the post World War II era.
RiPPs consist of any peptides (i.e. molecular weight below 10 kDa) that are ribosomally-produced and undergo some degree of enzymatic post-translational modification.This combination of peptide translation and modification is referred to as "post-ribosomal peptide synthesis" (PRPS) in analogy with nonribosomal peptide synthesis (NRPS).
The modifications produce MBL in multiple forms of slightly various molecular masses and pI from 5.7 to 6.2. [13] Proteolytic cleavage also resulted in removal of the 20-aa N-terminal signal peptide, [14] and hydroxylation and glycosylation were also detected. [13] Some cysteine residues can be converted to dehydroalanin. [15]