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Refinado por: Nome da Publicação: Biopolymers remover xxx: xxx remover
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1
Effect of methylene group insertions on the structural rigidity of Aib containing helices
Effect of methylene group insertions on the structural rigidity of Aib containing helices
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Effect of methylene group insertions on the structural rigidity of Aib containing helices

Duley, Anju ; Gowda, Vasantha ; Ganjiwale, Anjali ; Raghothama, Srinivasarao ; Ramanathan, Gurunath

Biopolymers, 2015-11, Vol.104 (6), p.720-732 [Periódico revisado por pares]

United States: Blackwell Publishing Ltd

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2
Crystal structures of peptide enantiomers and racemates: Probing conformational diversity in heterochiral Pro-Pro sequences
Crystal structures of peptide enantiomers and racemates: Probing conformational diversity in heterochiral Pro-Pro sequences
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Crystal structures of peptide enantiomers and racemates: Probing conformational diversity in heterochiral Pro-Pro sequences

Saha, Indranil ; Chatterjee, Bhaswati ; Shamala, Narayanaswamy ; Balaram, Padmanabhan

Biopolymers, 2008, Vol.90 (4), p.537-543 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

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3
Structural basis for the binding of high affinity phosphopeptides to Stat3
Structural basis for the binding of high affinity phosphopeptides to Stat3
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Structural basis for the binding of high affinity phosphopeptides to Stat3

McMurray, John S.

Biopolymers, 2008, Vol.90 (1), p.69-79 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

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4
Beta-branched residues adjacent to GG4 motifs promote the efficient association of glycophorin a transmembrane helices
Beta-branched residues adjacent to GG4 motifs promote the efficient association of glycophorin a transmembrane helices
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Beta-branched residues adjacent to GG4 motifs promote the efficient association of glycophorin a transmembrane helices

Cunningham, Fiona ; Poulsen, Bradley E. ; Ip, Wilfred ; Deber, Charles M.

Biopolymers, 2011, Vol.96 (3), p.340-347 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

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5
Combined effects of solvation and aggregation propensity on the final supramolecular structures adopted by hydrophobic, glycine-rich, elastin-like polypeptides
Combined effects of solvation and aggregation propensity on the final supramolecular structures adopted by hydrophobic, glycine-rich, elastin-like polypeptides
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Combined effects of solvation and aggregation propensity on the final supramolecular structures adopted by hydrophobic, glycine-rich, elastin-like polypeptides

Salvi, Anna M. ; Moscarelli, Pasquale ; Bochicchio, Brigida ; Lanza, Giuseppe ; Castle, James E.

Biopolymers, 2013-05, Vol.99 (5), p.292-313 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

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6
Influence of amino acid specificities on the molecular and supramolecular organization of glycine-rich elastin-like polypeptides in water
Influence of amino acid specificities on the molecular and supramolecular organization of glycine-rich elastin-like polypeptides in water
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Influence of amino acid specificities on the molecular and supramolecular organization of glycine-rich elastin-like polypeptides in water

Salvi, Anna M. ; Moscarelli, Pasquale ; Satriano, Giuseppina ; Bochicchio, Brigida ; Castle, James E.

Biopolymers, 2011-10, Vol.95 (10), p.702-721 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

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7
Chain length effects on helix-hairpin distribution in short peptides with Aib-DAla and Aib-Aib Segments
Chain length effects on helix-hairpin distribution in short peptides with Aib-DAla and Aib-Aib Segments
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Chain length effects on helix-hairpin distribution in short peptides with Aib-DAla and Aib-Aib Segments

Rajagopal, Appavu ; Aravinda, Subrayashastry ; Raghothama, Srinivasarao ; Shamala, Narayanaswamy ; Balaram, Padmanabhan

Biopolymers, 2011, Vol.96 (6), p.744-756 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

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8
VCD spectroscopic properties of the β-hairpin forming miniprotein CLN025 in various solvents
VCD spectroscopic properties of the β-hairpin forming miniprotein CLN025 in various solvents
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VCD spectroscopic properties of the β-hairpin forming miniprotein CLN025 in various solvents

Hatfield, Marcus P. D. ; Murphy, Richard F. ; Lovas, Sándor

Biopolymers, 2010-05, Vol.93 (5), p.442-450 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

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9
Tuning the β-turn segment in designed peptide β-hairpins: Construction of a stable type I′ β-turn nucleus and hairpin-helix transition promoting segments
Tuning the β-turn segment in designed peptide β-hairpins: Construction of a stable type I′ β-turn nucleus and hairpin-helix transition promoting segments
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Tuning the β-turn segment in designed peptide β-hairpins: Construction of a stable type I′ β-turn nucleus and hairpin-helix transition promoting segments

Rai, Rajkishor ; Raghothama, Srinivasarao ; Sridharan, Rajagopalan ; Balaram, Padmanabhan

Biopolymers, 2007, Vol.88 (3), p.350-361 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

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10
Simulated folding in polypeptides of diversified molecular tacticity: Implications for protein folding and de novo design
Simulated folding in polypeptides of diversified molecular tacticity: Implications for protein folding and de novo design
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Simulated folding in polypeptides of diversified molecular tacticity: Implications for protein folding and de novo design

Ramakrishnan, Vibin ; Ranbhor, Ranjit ; Durani, Susheel

Biopolymers, 2005-06, Vol.78 (2), p.96-105 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

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