Amide-to-ester substitution in coiled coils: The effect of removing hydrogen bonds on protein structure

Jessica A. Scheike; Carsten Baldauf; Jan Spengler; Fernando Albericio; M. Teresa Pisabarro; Beate Koksch

doi:10.1002/anie.200702218

Amide-to-ester substitution in coiled coils: The effect of removing hydrogen bonds on protein structure

Jessica A. Scheike
, Carsten Baldauf
, Jan Spengler
, Fernando Albericio
, M. Teresa Pisabarro
, Beate Koksch

Producción científica: Contribución a una revista › Artículo › revisión exhaustiva

38 Citas (Scopus)

Resumen

(Figure Presented) The latest twist: The effect of backbone H-bonding on the stability of proteins was studied by experimental techniques and molecular dynamics simulation. The structure of the coiled-coil model peptide examined (see picture) is affected by interactions in the solvent-exposed regions as well as by interhelical hydrophobic interactions.

Idioma original	Inglés
Páginas (desde-hasta)	7766-7769
Número de páginas	4
Publicación	Angewandte Chemie - International Edition
Volumen	46
N.º	41
DOI	https://doi.org/10.1002/anie.200702218
Estado	Publicada - 2007
Publicado de forma externa	Sí

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abstract = "(Figure Presented) The latest twist: The effect of backbone H-bonding on the stability of proteins was studied by experimental techniques and molecular dynamics simulation. The structure of the coiled-coil model peptide examined (see picture) is affected by interactions in the solvent-exposed regions as well as by interhelical hydrophobic interactions.",

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T1 - Amide-to-ester substitution in coiled coils

T2 - The effect of removing hydrogen bonds on protein structure

AU - Scheike, Jessica A.

AU - Baldauf, Carsten

AU - Spengler, Jan

AU - Albericio, Fernando

AU - Pisabarro, M. Teresa

AU - Koksch, Beate

PY - 2007

Y1 - 2007

N2 - (Figure Presented) The latest twist: The effect of backbone H-bonding on the stability of proteins was studied by experimental techniques and molecular dynamics simulation. The structure of the coiled-coil model peptide examined (see picture) is affected by interactions in the solvent-exposed regions as well as by interhelical hydrophobic interactions.

AB - (Figure Presented) The latest twist: The effect of backbone H-bonding on the stability of proteins was studied by experimental techniques and molecular dynamics simulation. The structure of the coiled-coil model peptide examined (see picture) is affected by interactions in the solvent-exposed regions as well as by interhelical hydrophobic interactions.

KW - Depsipeptides

KW - Hydrogen bonds

KW - Molecular dynamics

KW - Protein folding

KW - Superhelices

UR - https://www.scopus.com/pages/publications/35349013121

U2 - 10.1002/anie.200702218

DO - 10.1002/anie.200702218

M3 - Artículo

C2 - 17876795

AN - SCOPUS:35349013121

SN - 1433-7851

VL - 46

SP - 7766

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JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 41

ER -

Amide-to-ester substitution in coiled coils: The effect of removing hydrogen bonds on protein structure

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