Interruption of a 310-helix by a single Gly residue in a poly-Aib motif: A crystallographic study

Jordi Solà; Madeleine Helliwell; Jonathan Clayden

doi:10.1002/bip.21535

Interruption of a 310-helix by a single Gly residue in a poly-Aib motif: A crystallographic study

Jordi Solà
, Madeleine Helliwell
, Jonathan Clayden

Research output: Contribution to journal › Article › peer-review

Abstract

The structural influence of a single Gly residue inserted into an Aib16 homooligomer was studied in the solid state by X-ray crystallography. The peptides N3Aib8GlyAib8PheNH2 (1) and CbzPheAib8GlyAib8 (2) were found to adopt well-defined helical structures, which are broadly 310 helical. Indeed, 2 is the longest crystallographic 310 helix thus far reported. However, in the region of the central Gly residue, a loosening of the 310 structure is observed in both peptides, with 1 clearly showing local adoption of an α-helical structure in the region of residues 7-9. © 2010 Wiley Periodicals, Inc. Biopolymers 95: 62-69, 2011.

Original language	English
Pages (from-to)	62-69
Number of pages	7
Journal	Biopolymers
Volume	95
Issue number	1
DOIs	https://doi.org/10.1002/bip.21535
Publication status	Published - Jan 2011

Access to Document

10.1002/bip.21535

Cite this

@article{e91ee526e9384dee838b3d90c146ae92,

title = "Interruption of a 310-helix by a single Gly residue in a poly-Aib motif: A crystallographic study",

abstract = "The structural influence of a single Gly residue inserted into an Aib16 homooligomer was studied in the solid state by X-ray crystallography. The peptides N3Aib8GlyAib8PheNH2 (1) and CbzPheAib8GlyAib8 (2) were found to adopt well-defined helical structures, which are broadly 310 helical. Indeed, 2 is the longest crystallographic 310 helix thus far reported. However, in the region of the central Gly residue, a loosening of the 310 structure is observed in both peptides, with 1 clearly showing local adoption of an α-helical structure in the region of residues 7-9. {\textcopyright} 2010 Wiley Periodicals, Inc. Biopolymers 95: 62-69, 2011.",

author = "Jordi Sol{\`a} and Madeleine Helliwell and Jonathan Clayden",

year = "2011",

month = jan,

doi = "10.1002/bip.21535",

language = "English",

volume = "95",

pages = "62--69",

journal = "Biopolymers",

issn = "0006-3525",

publisher = "John Wiley \& Sons Ltd",

number = "1",

}

TY - JOUR

T1 - Interruption of a 310-helix by a single Gly residue in a poly-Aib motif: A crystallographic study

AU - Solà, Jordi

AU - Helliwell, Madeleine

AU - Clayden, Jonathan

PY - 2011/1

Y1 - 2011/1

N2 - The structural influence of a single Gly residue inserted into an Aib16 homooligomer was studied in the solid state by X-ray crystallography. The peptides N3Aib8GlyAib8PheNH2 (1) and CbzPheAib8GlyAib8 (2) were found to adopt well-defined helical structures, which are broadly 310 helical. Indeed, 2 is the longest crystallographic 310 helix thus far reported. However, in the region of the central Gly residue, a loosening of the 310 structure is observed in both peptides, with 1 clearly showing local adoption of an α-helical structure in the region of residues 7-9. © 2010 Wiley Periodicals, Inc. Biopolymers 95: 62-69, 2011.

AB - The structural influence of a single Gly residue inserted into an Aib16 homooligomer was studied in the solid state by X-ray crystallography. The peptides N3Aib8GlyAib8PheNH2 (1) and CbzPheAib8GlyAib8 (2) were found to adopt well-defined helical structures, which are broadly 310 helical. Indeed, 2 is the longest crystallographic 310 helix thus far reported. However, in the region of the central Gly residue, a loosening of the 310 structure is observed in both peptides, with 1 clearly showing local adoption of an α-helical structure in the region of residues 7-9. © 2010 Wiley Periodicals, Inc. Biopolymers 95: 62-69, 2011.

UR - https://www.ccdc.cam.ac.uk/structures/search?id=doi:10.5517/ccv60vw&sid=DataCite

U2 - 10.1002/bip.21535

DO - 10.1002/bip.21535

M3 - Article

SN - 0006-3525

VL - 95

SP - 62

EP - 69

JO - Biopolymers

JF - Biopolymers

IS - 1

ER -

Interruption of a 310-helix by a single Gly residue in a poly-Aib motif: A crystallographic study

Abstract

Access to Document

Other files and links

Fingerprint

Cite this