Large circular dichroism ellipticities for N-templated helical polypeptides are inconsistent with currently accepted helicity algorithms

Peter Wallimann; Robert J. Kennedy; Daniel S. Kemp

doi:10.1002/(SICI)1521-3773(19990503)38:9<1290::AID-ANIE1290>3.0.CO;2-E

Large circular dichroism ellipticities for N-templated helical polypeptides are inconsistent with currently accepted helicity algorithms

Peter Wallimann
, Robert J. Kennedy
, Daniel S. Kemp

Massachusetts Institute of Technology

Research output: Contribution to a Journal (Peer & Non Peer) › Article › peer-review

54 Citations (Scopus)

Abstract

An unprecedented, high degree of helicity as judged by CD spectroscopy is observed in N-templated model peptides of the type AcHel- (Ala₄Lys)(n)Ala₂-NH₂ (AcHel-Ala peptide pictured; AcHel is an N-terminal helix-inducing template for polypeptides). These results raise concern over the current methods for determining 100% helicity.

Original language	English
Pages (from-to)	1290-1292
Number of pages	3
Journal	Angewandte Chemie - International Edition
Volume	38
Issue number	9
DOIs	https://doi.org/10.1002/(SICI)1521-3773(19990503)38:9<1290::AID-ANIE1290>3.0.CO;2-E
Publication status	Published - 3 May 1999
Externally published	Yes

Keywords

Circular dichroism
Helical structures
Peptides

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10.1002/(SICI)1521-3773(19990503)38:9<1290::AID-ANIE1290>3.0.CO;2-E

Cite this

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title = "Large circular dichroism ellipticities for N-templated helical polypeptides are inconsistent with currently accepted helicity algorithms",

abstract = "An unprecedented, high degree of helicity as judged by CD spectroscopy is observed in N-templated model peptides of the type AcHel- (Ala4Lys)(n)Ala2-NH2 (AcHel-Ala peptide pictured; AcHel is an N-terminal helix-inducing template for polypeptides). These results raise concern over the current methods for determining 100\% helicity.",

keywords = "Circular dichroism, Helical structures, Peptides",

author = "Peter Wallimann and Kennedy, \{Robert J.\} and Kemp, \{Daniel S.\}",

year = "1999",

month = may,

day = "3",

doi = "10.1002/(SICI)1521-3773(19990503)38:9<1290::AID-ANIE1290>3.0.CO;2-E",

language = "English",

volume = "38",

pages = "1290--1292",

journal = "Angewandte Chemie - International Edition",

issn = "1433-7851",

publisher = "John Wiley and Sons Ltd",

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}

Large circular dichroism ellipticities for N-templated helical polypeptides are inconsistent with currently accepted helicity algorithms. / Wallimann, Peter; Kennedy, Robert J.; Kemp, Daniel S.
In: Angewandte Chemie - International Edition, Vol. 38, No. 9, 03.05.1999, p. 1290-1292.

Research output: Contribution to a Journal (Peer & Non Peer) › Article › peer-review

TY - JOUR

T1 - Large circular dichroism ellipticities for N-templated helical polypeptides are inconsistent with currently accepted helicity algorithms

AU - Wallimann, Peter

AU - Kennedy, Robert J.

AU - Kemp, Daniel S.

PY - 1999/5/3

Y1 - 1999/5/3

N2 - An unprecedented, high degree of helicity as judged by CD spectroscopy is observed in N-templated model peptides of the type AcHel- (Ala4Lys)(n)Ala2-NH2 (AcHel-Ala peptide pictured; AcHel is an N-terminal helix-inducing template for polypeptides). These results raise concern over the current methods for determining 100% helicity.

AB - An unprecedented, high degree of helicity as judged by CD spectroscopy is observed in N-templated model peptides of the type AcHel- (Ala4Lys)(n)Ala2-NH2 (AcHel-Ala peptide pictured; AcHel is an N-terminal helix-inducing template for polypeptides). These results raise concern over the current methods for determining 100% helicity.

KW - Circular dichroism

KW - Helical structures

KW - Peptides

UR - https://www.scopus.com/pages/publications/0033519313

U2 - 10.1002/(SICI)1521-3773(19990503)38:9<1290::AID-ANIE1290>3.0.CO;2-E

DO - 10.1002/(SICI)1521-3773(19990503)38:9<1290::AID-ANIE1290>3.0.CO;2-E

M3 - Article

AN - SCOPUS:0033519313

SN - 1433-7851

VL - 38

SP - 1290

EP - 1292

JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 9

ER -

Large circular dichroism ellipticities for N-templated helical polypeptides are inconsistent with currently accepted helicity algorithms

Abstract

Keywords

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