Unfolding of helical trans-β2,3-hybrid peptides with (α-β)nα composition, when executed by increasing solvent polarity or temperature, proceeded in a systematic manner with the turns unwinding sequentially; C-terminal region of these peptides were first to unwind and the process propagated towards N terminus with more and more β residues equilibrating from the gauche to the anti rotameric state across Cα£Cβ. This is evidenced by clear change in their CβH signal splitting, 3JCαH-CβH values, and sequential disappearance of i,i+2 NOEs. Helix-strand hybrid: Unfolding of helical trans-β2,3-hybrid peptides with (α-β)nα composition when executed by increasing solvent polarity or temperature, proceeded in a systematic manner with the turns unwinding sequentially; the C-terminal region of these peptides were first to unwind and the process propagated towards the N terminus with more and more β residues equilibrating from gauche to anti rotameric states across Cα£Cβ. © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Kannoth Manheri Muraleedharan

Department Of Chemistry

Amino acids

Protein folding

Solvents

C-TERMINAL REGIONS

CONFORMATIONAL TRANSITIONS

FOLDAMERS

HELICAL PEPTIDE

HELIX-STRAND HYBRID

HYBRID PEPTIDES

N TERMINUS

Solvent polarity

Peptides

amino acid

HELIX LOOP HELIX PROTEIN

peptide

solvent

chemical structure

chemistry

hydrogen bond

Nuclear magnetic resonance spectroscopy

protein conformation

HELIX-TURN-HELIX MOTIFS

Hydrogen Bonding

Magnetic Resonance Spectroscopy

Models, Molecular

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IIT Madras

Chemistry - A European Journal

A simple replacement of a H atom by Br transformed non-gelating aryl triazolyl amino acid benzyl ester into a versatile gelator, which formed shape-persistent, self-healing and mouldable gels. The ‘bromo-aryl benzyl ester' fragment was then transplanted into another framework, which resulted in similar solvent preference and gelation efficiency. © The Royal Society of Chemistry.

Chemical Communications

Towards a fragment-based approach in gelator design: halogen effects leading to thixotropic, mouldable and self-healing systems in aryl-triazolyl amino acid-based gelators!

A design approach that incorporates structural requirements for the formation of a 1D assembly, fibril stability, and fibril–fibril interactions for gelation was attempted by using amino acid-based sulfamides with the general structure Aa-NH-SO2-NH-Aa (Aa=amino acid). A preference for 1D assembly alone was not a sufficient condition for gelation, which became evident from studies involving sulfamide esters 1–5. Reducing the crystallization tendency without hindering unidirectional growth was executed through diacids of the sulfamide precursors with various amines that form an envelope around the sulfamide core through salt bridges. This strategy was fruitful, and gels of a wide variety of solvents could be formed by varying the acid and amine components. The use of dodecylamine or benzylamine, which could stabilize the molecular layers through alkylchain segregation or π–π interactions improved the gelation tendency, whereas the nature of the amino acid side chain, especially the rotational freedom and hydrophobicity, had a direct role in dictating the solvent preference. Crystallographic studies of these two-component systems gave molecular- level insight into the assembly and showed the importance of anisotropy in the distribution of secondary interactions in gelation. © 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

Sulfamide-lattice restructuring to form dimensionally controlled molecular arrays and gel-forming systems

The ability of α,β2,3-hybrid peptides with a heterochiral backbone to exist in a helical, extended, or partially folded state depending on the solvation conditions employed was investigated. The preference was found to be directly dictated by Cα-Cβ torsions in the β-residues. α,β-Hybrid peptides with a heterochiral backbone show the ability to exist in a helical, extended, or partially folded conformation depending on the solvation conditions employed. Copyright © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

European Journal of Organic Chemistry

Conformational Switching in Heterochiral α,β2,3-Hybrid Peptides in Response to Solvent Polarity

Anti or gauche? trans-β2,3-Amino acid residues that are known to promote extended structures in their peptides show specific rotamer preferences in response to an intramolecular hydrogen-bonding possibility, which facilitates the 11-helical structures in their 1:1 α,β-hybrid peptides (see figure). Preferences for the gauche conformation for all internal β residues and anti for the C-terminal residue in these peptides were confirmed by NMR spectroscopic and X-ray diffraction experiments. Copyright © 2012 WILEY-VCH Verlag GmbH &amp; Co. KGaA, Weinheim.

Unprecedented torsional preferences in trans-β2,3-amino acid residues and formation of 11-helices in α,β2,3-hybrid peptides

Plant, Soil and Environment

Vertisols and Cambisols had contrasting short term greenhouse gas responses to crop residue management

Biotropica

Reflections on tropical forest ecology from a forest giant

Homiletische Monatshefte

1. Weihnachtstag - 25. 12. 2014 Lukas 2,(1-14)15-20

Proceedings of the National Academy of Sciences

Effects of side chains in helix nucleation differ from helix propagation

Can Helical Peptides Unwind One Turn at a Time? - Controlled Conformational Transitions in α,β2,3-Hybrid Peptides

Journal	Data powered by TypesetChemistry - A European Journal
Publisher	Data powered by TypesetWiley-VCH Verlag
ISSN	09476539
Open Access	No