Mimicry of beta II'-turns of proteins in cyclic pentapeptides with one and without D-amino acids. (Q52979783)

10 May 2018

title

Mimicry of beta II'-turns of proteins in cyclic pentapeptides with one and without D-amino acids. (English)

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10 May 2018

author name string

H Weisshoff

1

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C Präsang

2

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P Henklein

3

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C Frömmel

4

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A Zschunke

5

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C Mügge

6

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language of work or name

English

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publication date

1 February 1999

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published in

FEBS Journal

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volume

259

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issue

3

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page(s)

776-788

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Emerging approaches in the molecular design of receptor-selective peptide ligands: conformational, topographical and dynamic considerations

cites work

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Cyclic pentapeptides as models for reverse turns: determination of the equilibrium distribution between type I and type II conformations of Pro-Asn and Pro-Ala beta-turns

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Arg-Gly-Asp constrained within cyclic pentapeptides. Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1.

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Multiple solution conformations of the integrin-binding cyclic pentapeptide cyclo(-Ser-D-Leu-Asp-Val-Pro-). Analysis of the (phi, psi) space available to cyclic pentapeptides

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Novel disulfide-constrained pentapeptides as models for beta-VIa turns in proteins

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Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units

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1-Hydroxy-7-azabenzotriazole. An efficient peptide coupling additive

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Cyclic Cholecystokinin-Analog Pentapeptide Cyclo (AsP-Trp-Met-AsP-Phe): An Unexpected Solution Conformation

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Calibration of the angular dependence of the amide proton-C alpha proton coupling constants, 3JHN alpha, in a globular protein. Use of 3JHN alpha for identification of helical secondary structure

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The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy

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Analysis and prediction of the different types of beta-turn in proteins

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Identifiers

DOI

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