Side-chain control of beta-peptide secondary structures. Design principles
نویسندگان
چکیده
منابع مشابه
Orientation of tyrosine side chain in neurotoxic Aβ differs in two different secondary structures of the peptide
Amyloid β (Aβ) peptide is present as a major component in amyloid plaque that is one of the hallmarks of Alzheimer's disease. The peptide contains a single tyrosine residue and Aβ has a major implication in the pathology of the disease progression. Current investigation revealed that the tyrosine side chain attained two different critical stereo orientations in two dissimilar conformational sta...
متن کاملinvestigating the feasibility of a proposed model for geometric design of deployable arch structures
deployable scissor type structures are composed of the so-called scissor-like elements (sles), which are connected to each other at an intermediate point through a pivotal connection and allow them to be folded into a compact bundle for storage or transport. several sles are connected to each other in order to form units with regular polygonal plan views. the sides and radii of the polygons are...
Design Principles of Length Control of Cytoskeletal Structures.
Cells contain elaborate and interconnected networks of protein polymers, which make up the cytoskeleton. The cytoskeleton governs the internal positioning and movement of vesicles and organelles and controls dynamic changes in cell polarity, shape, and movement. Many of these processes require tight control of the size and shape of cytoskeletal structures, which is achieved despite rapid turnov...
متن کاملPeptide ligation via side-chain auxiliary.
A new peptide ligation strategy based on a side-chain auxiliary was developed; the auxiliary is fairly simple and can be removed, without product isolation, under basic conditions.
متن کاملAnalysis of side-chain conformational distributions in neutrophil peptide-5 NMR structures.
The side-chain conformations have been analyzed in the antimicrobial peptide, Neutrophil Peptide-5 (NP-5), whose structure was independently generated from nmr-derived distance constraints using a distance geometry algorithm. The side-chain and peptide dihedral angle distributions in the nmr structures were compared with those constructed from a data base of high-resolution protein crystal stru...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 2003
ISSN: 0014-2956,1432-1033
DOI: 10.1046/j.1432-1033.2003.03756.x