A linear 23-residue peptide reveals a propensity to form an unusual native-like conformation

Simon Sherman, W. H. Gmeiner, L. Kirnarskiy, F. Perini, R. W. Ruddon

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

To gain insight into the earliest events of protein folding, a 23-residue peptide with a sequence corresponding to the 38-60 fragment of the β-subunit of human chorionic gonadotropin (hCGβ) was studied by NMR. In aqueous solution the majority of the peptide residues adopted an extended polyproline II (Pn) conformation similar to those in mature, fully folded hCGβ. The finding that the isolated protein fragment may acquire native-like structural motifs, even without α-helices or β-structures, extends the possibility of using free peptides as model systems to better understand the protein folding mechanisms. It was shown that the PII-rich structural motif can be determined efficiently by NMR spectroscopy. The observation that in the absence of extensive medium-and long-range interactions the majority of amino acid residues may adopt the PIIconformation suggests that the PII-rich structural motifs may play an important role in early events of protein folding.

Original languageEnglish (US)
Pages (from-to)441-446
Number of pages6
JournalJournal of Biomolecular Structure and Dynamics
Volume13
Issue number3
DOIs
StatePublished - Jan 1 1995

Fingerprint

Protein Folding
Chorionic Gonadotropin
Peptides
Magnetic Resonance Spectroscopy
Amino Acids
Proteins

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

Cite this

A linear 23-residue peptide reveals a propensity to form an unusual native-like conformation. / Sherman, Simon; Gmeiner, W. H.; Kirnarskiy, L.; Perini, F.; Ruddon, R. W.

In: Journal of Biomolecular Structure and Dynamics, Vol. 13, No. 3, 01.01.1995, p. 441-446.

Research output: Contribution to journalArticle

Sherman, Simon ; Gmeiner, W. H. ; Kirnarskiy, L. ; Perini, F. ; Ruddon, R. W. / A linear 23-residue peptide reveals a propensity to form an unusual native-like conformation. In: Journal of Biomolecular Structure and Dynamics. 1995 ; Vol. 13, No. 3. pp. 441-446.
@article{8b1b80b9be0041aea89862361783012c,
title = "A linear 23-residue peptide reveals a propensity to form an unusual native-like conformation",
abstract = "To gain insight into the earliest events of protein folding, a 23-residue peptide with a sequence corresponding to the 38-60 fragment of the β-subunit of human chorionic gonadotropin (hCGβ) was studied by NMR. In aqueous solution the majority of the peptide residues adopted an extended polyproline II (Pn) conformation similar to those in mature, fully folded hCGβ. The finding that the isolated protein fragment may acquire native-like structural motifs, even without α-helices or β-structures, extends the possibility of using free peptides as model systems to better understand the protein folding mechanisms. It was shown that the PII-rich structural motif can be determined efficiently by NMR spectroscopy. The observation that in the absence of extensive medium-and long-range interactions the majority of amino acid residues may adopt the PIIconformation suggests that the PII-rich structural motifs may play an important role in early events of protein folding.",
author = "Simon Sherman and Gmeiner, {W. H.} and L. Kirnarskiy and F. Perini and Ruddon, {R. W.}",
year = "1995",
month = "1",
day = "1",
doi = "10.1080/07391102.1995.10508853",
language = "English (US)",
volume = "13",
pages = "441--446",
journal = "Journal of Biomolecular Structure and Dynamics",
issn = "0739-1102",
publisher = "Adenine Press",
number = "3",

}

TY - JOUR

T1 - A linear 23-residue peptide reveals a propensity to form an unusual native-like conformation

AU - Sherman, Simon

AU - Gmeiner, W. H.

AU - Kirnarskiy, L.

AU - Perini, F.

AU - Ruddon, R. W.

PY - 1995/1/1

Y1 - 1995/1/1

N2 - To gain insight into the earliest events of protein folding, a 23-residue peptide with a sequence corresponding to the 38-60 fragment of the β-subunit of human chorionic gonadotropin (hCGβ) was studied by NMR. In aqueous solution the majority of the peptide residues adopted an extended polyproline II (Pn) conformation similar to those in mature, fully folded hCGβ. The finding that the isolated protein fragment may acquire native-like structural motifs, even without α-helices or β-structures, extends the possibility of using free peptides as model systems to better understand the protein folding mechanisms. It was shown that the PII-rich structural motif can be determined efficiently by NMR spectroscopy. The observation that in the absence of extensive medium-and long-range interactions the majority of amino acid residues may adopt the PIIconformation suggests that the PII-rich structural motifs may play an important role in early events of protein folding.

AB - To gain insight into the earliest events of protein folding, a 23-residue peptide with a sequence corresponding to the 38-60 fragment of the β-subunit of human chorionic gonadotropin (hCGβ) was studied by NMR. In aqueous solution the majority of the peptide residues adopted an extended polyproline II (Pn) conformation similar to those in mature, fully folded hCGβ. The finding that the isolated protein fragment may acquire native-like structural motifs, even without α-helices or β-structures, extends the possibility of using free peptides as model systems to better understand the protein folding mechanisms. It was shown that the PII-rich structural motif can be determined efficiently by NMR spectroscopy. The observation that in the absence of extensive medium-and long-range interactions the majority of amino acid residues may adopt the PIIconformation suggests that the PII-rich structural motifs may play an important role in early events of protein folding.

UR - http://www.scopus.com/inward/record.url?scp=0029609883&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029609883&partnerID=8YFLogxK

U2 - 10.1080/07391102.1995.10508853

DO - 10.1080/07391102.1995.10508853

M3 - Article

VL - 13

SP - 441

EP - 446

JO - Journal of Biomolecular Structure and Dynamics

JF - Journal of Biomolecular Structure and Dynamics

SN - 0739-1102

IS - 3

ER -