Helix-coil transition of the isolated amino terminus of ribonuclease

Brown, James Edward; Klee, Werner A.

doi:10.1021/bi00779a019

Cited by 312 publications

(166 citation statements)

References 16 publications

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“…These results were entirely consistent with previous studies by Brown and Klee, 141 Kim and Baldwin, 142 and Nelson and Kallenbach 143 that showed that S-peptide had a nascent ahelical segment that could be stabilized by experimental conditions. …”

Section: Dynamics and Enzyme Mechanismsupporting

confidence: 92%

Back to the future: Ribonuclease A

2008

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Pancreatic ribonuclease A (EC 3.1.27.5, RNase) is, perhaps, the best‐studied enzyme of the 20th century. It was isolated by René Dubos, crystallized by Moses Kunitz, sequenced by Stanford Moore and William Stein, and synthesized in the laboratory of Bruce Merrifield, all at the Rockefeller Institute/University. It has proven to be an excellent model system for many different types of experiments, both as an enzyme and as a well‐characterized protein for biophysical studies. Of major significance was the demonstration by Chris Anfinsen at NIH that the primary sequence of RNase encoded the three‐dimensional structure of the enzyme. Many other prominent protein chemists/enzymologists have utilized RNase as a dominant theme in their research. In this review, the history of RNase and its offspring, RNase S (S‐protein/S‐peptide), will be considered, especially the work in the Merrifield group, as a preface to preliminary data and proposed experiments addressing topics of current interest. These include entropy–enthalpy compensation, entropy of ligand binding, the impact of protein modification on thermal stability, and the role of protein dynamics in enzyme action. In continuing to use RNase as a prototypical enzyme, we stand on the shoulders of the giants of protein chemistry to survey the future. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 90: 259–277, 2008.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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Section: Dynamics and Enzyme Mechanismsupporting

confidence: 92%

Back to the future: Ribonuclease A

2008

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“…3 Since the discovery of significant helicity in the 13 amino acid C-peptide from ribonuclease A, 4,5 there has been a considerable amount of research on helicity of de novo peptides. Peptides ranging from 12 to 30 residues have been studied to understand the interplay between side chain interactions, the helix dipole, and the intrinsic helix-forming ability of each amino acid.…”

Section: Introductionmentioning

confidence: 99%

Helicity of short E‐R/K peptides

et al. 2010

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Understanding the secondary structure of peptides is important in protein folding, enzyme function, and peptide-based drug design. Previous studies of synthetic Ala-based peptides (>12 a.a.) have demonstrated the role for charged side chain interactions involving Glu/Lys or Glu/Arg spaced three (i, i 1 3) or four (i, i 1 4) residues apart. The secondary structure of short peptides (<9 a.a.), however, has not been investigated. In this study, the effect of repetitive Glu/Lys or Glu/Arg side chain interactions, giving rise to E-R/K helices, on the helicity of short peptides was examined using circular dichroism. Short E-R/K-based peptides show significant helix content. Peptides containing one or more E-R interactions display greater helicity than those with similar E-K interactions. Significant helicity is achieved in Arg-based E-R/K peptides eight, six, and five amino acids long. In these short peptides, each additional i 1 3 and i 1 4 salt bridge has substantial contribution to fractional helix content. The E-R/K peptides exhibit a strongly linear melt curve indicative of noncooperative folding. The significant helicity of these short peptides with predictable dependence on number, position, and type of side chain interactions makes them an important consideration in peptide design.

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“…The helix problem languished for 11 years, perhaps because of the disappointing results found in the laboratories of Anfinsen and Scheraga. In 1982, Bierzynski et al [87] used NMR as well as CD spectroscopy to reinvestigate the claim of Brown and Klee [86] and confirmed that partial helix formation occurs. Bierzynski et al found that helix formation is strongly pH dependent and the pK values indicate that both a His residue and a Glu residue are required for helix formation, thus implicating specific side-chain interactions [87].…”

Section: Historymentioning

confidence: 99%

“…In 1969 Taniuchi and Anfinsen [84] cleaved staphylococcal nuclease, which has 149 residues, between residues 126 and 127 and found that both fragments 1-126 and 127-149 (each of which has a helix of modest size) were structureless by CD as well as by other physical criteria. In 1969-1971 Klee obtained tantalizing results, suggestive of some helix formation at low temperatures, with the ''S-peptide'' (residues 1-20) [85] and ''C-peptide'' (residues 1-13) [86] of ribonuclease A. (The RNase A helix contains residues 3-12.)…”

Section: Historymentioning

confidence: 99%

Weak Interactions in Protein Folding: Hydrophobic Free Energy, van der Waals Interactions, Peptide Hydrogen Bonds, and Peptide Solvation

Baldwin¹

2005

Protein Folding Handbook

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Helix-coil transition of the isolated amino terminus of ribonuclease

Cited by 312 publications

References 16 publications

Back to the future: Ribonuclease A

Back to the future: Ribonuclease A

Helicity of short E‐R/K peptides

Weak Interactions in Protein Folding: Hydrophobic Free Energy, van der Waals Interactions, Peptide Hydrogen Bonds, and Peptide Solvation

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