Amide proton exchange rates of oxidized and reduced saccharomyces cerevisiae iso‐1‐cytochrome c

Protein Science

Volumn 2, Issue 11, 1993, Pages 1966-1974

  Marmorino, Jennifer L ^a   Auld, Douglas S ^a,b   Betz, Stephen F ^a,c   Doyle, Donald F ^a   Young, Gregory B ^a   Pielak, Gary J ^a  

^a UNIVERSITY OF NORTH CAROLINA   (United States)

^b MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^c DUPONT COMPANY   (United States)

Author keywords

amide proton exchange; cytochrome c; denaturation; NMR; protein stability

Indexed keywords

CYTOCHROME C;

ARTICLE; DENATURATION; HYDROGEN BOND; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SACCHAROMYCES CEREVISIAE;

SACCHAROMYCES CEREVISIAE;

EID: 0027495048     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.5560021118     Document Type: Article

References (53)

1. Constraints on amino acid substitutions in the N‐terminal helix of cytochrome c explored by random mutagenesis
2. Primary structure effects on peptide group hydrogen exchange
3. Oxidation state‐dependent conformational changes in cytochrome c.
4. Introduction of a disulfide bond into cytochrome c stabilizes a compact denatured state
5. Electrochemical probes of protein folding
6. Isotope effects in peptide group hydrogen exchange
7. Replacement of cysteine‐107 of Saccharomyces cerevisiae iso‐1‐cytochrome c with threonine: Improved stability of the mutant protein
8. Hydrogen‐tritium exchange kinetics of soybean trypsin inhibitor (Kunitz). Solvent accessibility on the folded conformation
9. Measurement and calibration of peptide group hydrogen‐deuterium exchange by ultraviolet spectrophotometry
10. Hydrogen exchange and structural dynamics of proteins and nucleic acids
11. Redox‐dependent structure change and hyperfine nuclear magnetic resonance shifts in cytochrome c.
12. Deletion and replacements of omega loops in yeast iso‐1‐cytochrome c.
13. Loops in globular proteins: A novel category of secondary structure
14. Exploring the interface between the N‐ and C‐terminal helices of cytochrome c by random mutagenesis within the C‐terminal helix
15. Comparison of reduced and oxidized yeast iso‐1‐cytochrome c using paramagnetic shifts
16. Assignment of proton resonances, identification of secondary structural elements, and analysis of backbone chemical shifts for the C102T variant of yeast iso‐1‐cytochrome c and horse cytochrome c.
17. Use of glass electrodes to measure acidities in deuterium oxide
18. 15N NMR study
19. Water catalysis of peptide hydrogen isotope exchange
20. Dramatic stabilization of ferricytochrome c upon reduction
21. Hydrogen exchange in proteins
22. Residual helical structure in the C‐terminal fragment of cytochrome c.
23. The interpretation of protein structures: Estimation of static accessibility
24. On the theory of the helix‐coil transition in polypeptides
25. Deuterium exchange and protein structure
26. High‐resolution refinement of yeast iso‐1‐cytochrome c and comparisons with other eukaryotic cytochromes c.
27. Yeast iso‐1‐cytochrome c. A 2.8 Å resolution three‐dimensional structure determination
28. 1H spin‐spin coupling constants in proteins
29. Effect of antibody binding on protein motions studied by hydrogen‐exchange labeling and two‐dimensional NMR
30. Proton magnetic resonance studies of horse cytochrome c.
31. Primary structure effects on peptide group hydrogen exchange
32. The properties and functions of tryptophan in proteins
33. Effective concentrations of amino acid side chains in an unfolded protein
34. Nuclear magnetic resonance studies of slowly exchanging peptide protons in cytochrome c in aqueous solution
35. An antibody binding site on cytochrome c defined by hydrogen exchange and two‐dimensional NMR
36. 2 of the Linderstrøm‐Lang model for protein amide hydrogen exchange: A study of the individual amides in hen egg‐white lysozyme
37. Proton exchange in amides: Surprises from simple systems
38. Hydrogen exchange in native and denatured states of hen egg‐white lysozyme
39. 2H and temperature
40. Turns in peptides and proteins
41. The mutational alteration of the primary structure of yeast iso‐1‐cytochrome c.
42. GEPOL: An improved description of molecular surfaces II. Computing the molecular area and volume
43. Conformational change in cytochrome c. II. Ferricytochrome c refinement at 1.8 Å and comparison with the ferrocytochrome c structure
44. Hydrogen exchange in Pseudomonas cytochrome c‐551
45. 1H NMR studies of cytochrome c: Hydrogen exchange in the N‐terminal helix
46. Comparison of the solution and crystal structures of mitochondrial cytochrome c: Analysis of the paramagnetic shifts in the nuclear magnetic resonance spectrum of ferricytochrome c.
47. Hydrogen exchange kinetics and internal motions in proteins and nucleic acids
48. 2
49. 1H NMR
50. Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
51. Theory of the phase transition between helix and random coil in polypeptide chains