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141.
We identify a distinctive circular dichroism (CD) signature for self-assembled 14-helical beta-peptides. Our data show that self-assembly leads to a mimimum at 205 nm, which is distinct from the well-known minimum at 214 nm for a monomeric 14-helix. The onset of assembly is indicated by [theta]205/[theta]214>0.7. Our results will facilitate rapid screening for self-assembling beta-peptides and raise the possibility that far-UV CD will be useful for detecting higher-order structure for other well-folded oligoamide backbones. 相似文献
142.
The reaction of chlorosulfonyl isocyanate (CSI) with alkenes provides beta-lactams in quantity, and the products have frequently been used for ring-opening polymerization to generate nylon-3 materials. Prior uses of this approach have focused almost entirely on beta-lactams with purely hydrocarbon substitutents. We show how a variety of beta-lactams bearing protected polar substituents can be generated from CSI-derived building blocks. 相似文献
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Prof. Pil Seok Chae Prof. Søren G. F. Rasmussen Rohini R. Rana Kamil Gotfryd Andrew C. Kruse Aashish Manglik Kyung Ho Cho Shailika Nurva Prof. Ulrik Gether Prof. Lan Guan Prof. Claus J. Loland Dr. Bernadette Byrne Prof. Brian K. Kobilka Prof. Samuel H. Gellman 《Chemistry (Weinheim an der Bergstrasse, Germany)》2012,18(31):9434-9434
148.
Improved Glucose‐Neopentyl Glycol (GNG) Amphiphiles for Membrane Protein Solubilization and Stabilization 下载免费PDF全文
Kyung Ho Cho Hyoung Eun Bae Dr. Manabendra Das Prof. Samuel H. Gellman Prof. Pil Seok Chae 《化学:亚洲杂志》2014,9(2):632-638
Membrane proteins are inherently amphipathic and undergo dynamic conformational changes for proper function within native membranes. Maintaining the functional structures of these biomacromolecules in aqueous media is necessary for structural studies but difficult to achieve with currently available tools, thus necessitating the development of novel agents with favorable properties. This study introduces several new glucose‐neopentyl glycol (GNG) amphiphiles and reveals some agents that display favorable behaviors for the solubilization and stabilization of a large, multi‐subunit membrane protein assembly. Furthermore, a detergent structure–property relationship that could serve as a useful guideline for the design of novel amphiphiles is discussed. 相似文献
149.
Clemens Mayer Dr. Manuel M. Müller Prof. Dr. Samuel H. Gellman Prof. Dr. Donald Hilvert 《Angewandte Chemie (International ed. in English)》2014,53(27):6978-6981
Foldamers are non‐natural oligomers that adopt stable conformations reminiscent of those found in proteins. To evaluate the potential of foldameric subunits for catalysis, semisynthetic enzymes containing foldamer fragments constructed from α‐ and β‐amino acid residues were designed and characterized. Systematic variation of the α→β substitution pattern and types of β‐residue afforded highly proficient hybrid catalysts, thus demonstrating the feasibility of expanding the enzyme‐engineering toolkit with non‐natural backbones. 相似文献
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Dr. Zhen Yu Dr. Dale F. Kreitler Yin Ting T. Chiu Ruiwen Xu Austin T. Bruchs Dr. Craig A. Bingman Prof. Samuel H. Gellman 《Angewandte Chemie (International ed. in English)》2023,62(40):e202308100
Peptide engineering efforts have delivered drugs for diverse human diseases. Side chain alteration is among the most common approaches to designing new peptides for specific applications. The peptide backbone can be modified as well, but this strategy has received relatively little attention. Here we show that new and favorable contacts between a His side chain on a target protein and an aromatic side chain on a synthetic peptide ligand can be engineered by rational and coordinated side chain modification and backbone extension. Side chain modification alone was unsuccessful. Binding measurements, high-resolution structural studies and pharmacological outcomes all support the synergy between backbone and side chain modification in engineered ligands of the parathyroid hormone receptor-1, which is targeted by osteoporosis drugs. These results should motivate other structure-based designs featuring coordinated side chain modification and backbone extension to enhance the engagement of peptide ligands with target proteins. 相似文献