Identifying a folding nucleus for the lysozyme/α-lactalbumin family from sequence conservation clusters

Journal of Molecular Evolution

Volumn 54, Issue 4, 2002, Pages 425-436

  Ting, Kai Li H ^a   Jernigan, Robert L ^a  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

"Fast track" pathway; Lactalbumin; Consensus conservation; Folding nucleus; Lysozyme; Phylogenetic

Indexed keywords

ALPHA LACTALBUMIN; LYSOZYME;

ALPHA HELIX; ARTICLE; BETA CHAIN; ENZYME STRUCTURE; GENE CLUSTER; GENE SEQUENCE; GENETIC CONSERVATION; PHYLOGENY; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING;

AMINO ACID SEQUENCE; ANIMALS; CONSERVED SEQUENCE; EVOLUTION, MOLECULAR; LACTALBUMIN; MOLECULAR SEQUENCE DATA; MULTIGENE FAMILY; MURAMIDASE; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT;

EID: 0036218061     PISSN: 00222844     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00239-001-0033-x     Document Type: Article

References (67)

1. Refined structure of baboon alpha-lactalbumin at 1.7 A resolution
2. Rapid formation of a molten globule intermediate in refolding of α-lactalbumin
3. Role of the molten globule state in protein folding
4. Refinement of human lysozyme at 1.5 angstrom resolution analysis of non-bonded and hydrogen-bond interactions
5. Pulsed H/D-exchange studies of folding intermediates
6. Characterizing protein folding intermediates
7. Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea pig α-lactalbumin
8. Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Å resolution
9. Comparison of the amino acid sequence of bovine α-lactalbumin and hen's egg white lysozyme
10. A partially folded state of hen egg white lysozyme in trifluoroethanol: Structural characterization and implications for protein folding
11. Kinetic resolution of peptide bond and side chain far-UV circular dichroism during the folding of hen egg white lysozyme
12. Three dimensional structure of a heteroclitic antigen-antibody cross-reaction complex
13. Folding kinetics of vilin 14T, a protein domain with a central β-sheet and two hydrophobic cores
14. Differential stabilization of two hydrophobic cores in the transition state of the vilin 14T folding reaction
15. Understanding protein folding via free-energy surfaces from theory and experiment
16. The molten globule protein conformation probed by disulphide bonds
17. Pathway of disulfide-coupled unfolding and refolding of bovine alpha-lactalbumin
18. Analysis of catalytic properties of hen egg white lysozyme during renaturation from denatured and reduced material
19. Changes in the apomyoglobin folding pathway caused by mutation of the distal histine residue
20. Structure-based analysis of protein dynamics: Comparison of theoretical results for hen lysozyme with X-ray diffraction and NMR relaxation data
21. Structural characterization of a partly folded apomyoglobin intermediate
22. Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: A comparative study of the folding reactions of alpha-lactalbumin and lysozyme
23. Insect lysozyme from house fly (musca domestica) larvae: Possible digestive function based on sequence and enzymatic properties
24. a of His-24 in the folding transition state of apomyoglobin
25. Formation of molten globule intermediate early in the kinetic folding pathway of apomyoglobin
26. Direct measurement of nucleation and growth rates in lysozyme folding
27. Comparison of the transient folding intermediates in lysozyme alpha-lactalbumin
28. 2+ binding on the folding kinetics of α-lactalbumin
29. Are there pathways in protein folding?
30. How Ala→Gly mutations in different helices affect the stability of the apomyoglobin molten globule
31. Dissection of protein-carbohydrate interactions in mutant hen egg-white lysozyme complexes and their hydrolytic activity
32. Fast and slow tracks in lysozyme folding: Insight into the role of domains in the folding process
33. Demonstration by NMR of folding domains in lysozyme
34. Universally conserved positions in protein folds: Reading evolutionary signals about stability, folding kinetics and function
35. Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy
36. Structural basis of the stability of a lysozyme molten globule
37. Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants
38. An analysis of protein pathway
39. Folding of tryptophan mutants of barstar: Evidence for an initial hydrophobic collapse on the folding pathway
40. Crystallographic studies of lysozyme and its interactions with inhibitors and substrates
41. Crystal structures of guinea-pig, goat and bovine alpha-lactalbumin significant for its action in lactose synthase
42. Thermodynamic parameters of helix-coil transition in polypeptide chains
43. The stepwise mechanism of protein molecule self-organization
44. Protein folding and protein evolution: Common folding nucleus in different subfamilies of c-type cytochromes?
45. Non-functional conserved residues in globins and their possible role as a folding nucleus
46. Molecular divergence of lysozymes and α-lactalbumin
47. The folding of hen lysozyme involves partially structured intermediates and multiple pathways
48. α-Lactalbumin forms a compact molten globule in the absence of disulfide bonds
49. Alpha-lactalbumin possesses a distinct zinc binding site
50. Structural characterization of folding intermediates in cytochrome c by H-D exchange labelling and proteion NMR
51. Extracting information on folding from the amino acid sequence: Consensus regions with preferred conformation in homologues proteins
52. Studies of L-canavanine incorporation into insectan lysozyme
53. Proline scanning mutagenesis of a molten globule reveals non-cooperative formation of a protein's overall topology
54. Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human alpha-lactalbumin
55. A residue-specific NMR view of the non-cooperative unfolding of a molten globule
56. Conserved residues and the mechanism of protein folding
57. α-Lactalbumin possesses a novel calcium binding loop
58. Conformational comparison between α-lactalbumin and lysozyme
59. Molten globule versus variety of intermediates: Influence of anions on pH-denatured apomyoglobin
60. Nanosecond dynamics of the single tryptophan reveals multi-state equilibrium unfolding of protein GB1
61. Chimeras of human lysozyme and α-lactalbumin: An interesting tool for studying partially folded states during protein folding
62. Structural studies on the binding of 4-methylhunbelliferone glycosides of rainbow trout lysozyme
63. The refined structures of goose lysozyme and its complex with bound trisaccharide show that the goose type lysozymes lack a catalytic aspartate
64. A specific hydrophobic core in the α-lactalbumin molten globule
65. Bipartite structure of the α-lactalbumin molten globule
66. NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding