Conformational switching in designed peptides: the helix/sheet transition (Q44712177)

5 December 2017

title

Conformational switching in designed peptides: the helix/sheet transition (English)

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5 December 2017

2

Cohen FE

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5 December 2017

Cerpa R

1

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5 December 2017

Kuntz ID

series ordinal

3

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5 December 2017

publication date

1 January 1996

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5 December 2017

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5 December 2017

volume

1

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5 December 2017

issue

2

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5 December 2017

page(s)

91-101

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The far ultraviolet absorption spectra of polypeptide and protein solutions and their dependence on conformation

5 December 2017

cites work

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On the use of sequence homologies to predict protein structure: identical pentapeptides can have completely different conformations

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Origins of structural diversity within sequentially identical hexapeptides

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Importance of environment in determining secondary structure in proteins

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Environment affects amino acid preference for secondary structure

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NMR studies of amyloid beta-peptides: proton assignments, secondary structure, and mechanism of an alpha-helix----beta-sheet conversion for a homologous, 28-residue, N-terminal fragment

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7 January 2021

Prion protein peptides induce alpha-helix to beta-sheet conformational transitions

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7 January 2021

Studies of synthetic helical peptides using circular dichroism and nuclear magnetic resonance

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7 January 2021

Tests of the helix dipole model for stabilization of α-helices

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7 January 2021

Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design

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7 January 2021

Design and characterization of peptides with amphiphilic beta-strand structures

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Unusually stable beta-sheet formation in an ionic self-complementary oligopeptide

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Primary structure elements responsible for the conformational switch in the envelope glycoprotein gp120 from human immunodeficiency virus type 1: LPCR is a motif governing folding

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7 January 2021

Surface-induced conformational switching in amphiphilic peptide segments of apolipoproteins B and E and model peptides

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7 January 2021

Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities

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Circular dichroism studies of barnase and its mutants: characterization of the contribution of aromatic side chains

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Computed circular dichroism spectra for the evaluation of protein conformation

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Circular dichroism studies of distorted alpha-helices, twisted beta-sheets, and beta turns

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Beta-structure in human amylin and two designer beta-peptides: CD and NMR spectroscopic comparisons suggest soluble beta-oligomers and the absence of significant populations of beta-strand dimers

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Ultrafast infrared spectroscopy

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7 January 2021

10.1016/S1359-0278(96)00018-1

Identifiers

DOI

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5 December 2017

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