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Properties of de novo designed helical proteins. A Monte Carlo study of degrado dimers

โœ Scribed by Andrzej Sikorski

Book ID
108314238
Publisher
Elsevier Science
Year
1999
Tongue
English
Weight
29 KB
Volume
121-122
Category
Article
ISSN
0010-4655

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๐Ÿ“œ SIMILAR VOLUMES

Computer simulations of the properties o
Computer simulations of the properties of the ฮฑ2, ฮฑ2C, and ฮฑ2D de novo designed helical proteins
โœ Andrzej Sikorski; Andrzej Kolinski; Jeffrey Skolnick ๐Ÿ“‚ Article ๐Ÿ“… 2000 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 286 KB ๐Ÿ‘ 1 views

Reduced lattice models of the three de novo designed helical proteins โฃ 2 , โฃ 2 C, and โฃ 2 D were studied. Low temperature stable folds were obtained for all three proteins. In all cases, the lowest energy folds were four-helix bundles. The folding pathway is qualitatively the same for all proteins

Fmoc-based synthesis of glycolate ester
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โœ Daniel J Suich; Marcus D Ballinger; James A Wells; William F DeGrado ๐Ÿ“‚ Article ๐Ÿ“… 1996 ๐Ÿ› Elsevier Science ๐ŸŒ French โš– 320 KB

An automated method utilizing Fmoc-protected amino acids has been developed for the synthesis of glycolate ester peptides as substrates for subtiligase. As a test of this methodology, peptide esters containing o-helical sequences that specify the association into 3-and 4helix bundles were synthesize