Analysis of the segmental stability of helical peptides by isotope-edited infrared spectroscopy

Proteins: Structure, Function and Genetics

Volumn 45, Issue 1, 2001, Pages 81-89

  Parker, James S ^a   Mizuguchi, Kenji ^a   Gay, Nicholas J ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Circular dichroism; Helical peptide; Infrared spectra; Isotope labeling; Segmental stability; Temperature dependence

Indexed keywords

ALANINE; ISOTOPE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; INFRARED SPECTROSCOPY; ISOTOPE LABELING; PRIORITY JOURNAL; PROTEIN STABILITY; TEMPERATURE DEPENDENCE;

ALANINE; AMINO ACID SEQUENCE; CIRCULAR DICHROISM; ISOTOPE LABELING; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; SPECTROPHOTOMETRY, INFRARED; THERMODYNAMICS;

EID: 0035479710     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.1126     Document Type: Article

References (36)

1. Design of α-helical peptides: Their role in protein folding and molecular biology
2. Helix geometry in proteins
3. + salt bridges in short peptides of de novo design
4. Measuring the strength of side-chain hydrogen bonds in peptide helices: The Gln Asp (i, i + 4) interaction
5. Modulation of the helical stability of a model peptides by ionic residues
6. A model peptide with enhanced helicity
7. Incorporation of pairwise interactions into the Lifson-Roig model for helix prediction
8. 13C NMR
9. Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
10. Fast events in protein folding: Relaxation dynamics and structure of the I form of apomyoglobin
11. Fast events in protein folding: Helix melting and formation in small peptide
12. The effects of chain length and thermal denaturation on helix-forming peptides: A mode-specific analysis using 2D FT-IR
13. Isotope-edited Fourier transform infrared spectroscopy studies of calmodulin's interaction with its target peptides
14. Isotope-edited infrared spectroscopy of helical peptides
15. Effect of hexafluoroisopropanol on the thermodynamics of peptide secondary structure formation
16. -1 range and quantitative infrared spectroscopy of aqueous solutions
17. Computed circular dichroism spectra for the evaluation of protein conformation
18. 2O) solutions. II. Amide absorption bands of polypeptides and fibrous proteins in α-, β-, and random coil conformation
19. Intensities and other spectral parameters of infrared amide bands of polypeptides in the α-helical form
20. Intensities and other spectral parameters of infrared amide bands of polypeptides in the β- and random forms
21. Heat capacity and conformation of proteins in the denatured state
22. Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solution in heavy water
23. The two-dimensional IR nonlinear spectroscopy of a cyclic penta-peptide in relation to its three-dimensional structure
24. 2O) solutions. I. Spectral parameters of amino acid residue absorption bands
25. The infrared absorption of amino acid side chains
26. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
27. 2O) solutions. III. Estimation of the protein secondary structure
28. Estimation of the number of α-helical and β-strand segments in proteins using circular dichroism spectroscopy
29. Infrared spectra and resonance interactions of amide-I and II vibrations of α-helix
30. Experimental molecular dynamics of an alanine-base helical peptide determined by spin label electron spin resonance
31. Site-specific conformational determination in thermal unfolding studies of helical peptides using vibrational circular dichroism with isotopic substitution
32. Unfolding of an α-helix in water
33. Molecular dynamics simulations of the unfolding of an α-helical analogue of ribonuclease A S-peptide in water
34. Molecular dynamics analysis of a ribonuclease C-peptide analogue
35. 10: The split personality of polypeptide helices
36. Standard structures in proteins