Functional and structural roles of constituent amino acid residues of bovine pancreatic ribonuclease A

Journal of Bioscience and Bioengineering

Volumn 92, Issue 2, 2001, Pages 98-107

  Chatani, Eri ^a   Hayashi, Rikimaru ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

Active site; Amino acid residues; Protein engineering; RNase A; Structure

Indexed keywords

CONFORMATIONS; DATA ACQUISITION; MOLECULES; PROTEINS; RNA;

BOVINE PANCREAS;

AMINO ACIDS;

AMINO ACID; PANCREATIC RIBONUCLEASE;

AMINO ACID SEQUENCE; CATTLE; CHEMICAL BINDING; CHEMICAL MODIFICATION; ENZYME ACTIVE SITE; GENETIC ENGINEERING; NONHUMAN; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; REVIEW; X RAY CRYSTALLOGRAPHY;

BOS TAURUS; BOVINAE;

EID: 0034846953     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1263/jbb.92.98     Document Type: Review

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9. On the alkylation of amino acid residues at the active site of ribonuclease
10. Tertiary structure of ribonuclease
11. Structure of ribonuclease
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14. On the mechanism of action of ribonuclease A: Relevance of enzymatic studies with a p-nitrophenylphosphate ester and a thiophosphate ester
15. Crystal structure of ribonuclease A-d (ApTpApApG) complex. Direct evidence for extended substrate recognition
16. The mechanism of binding of a polynucleotide chain to pancreatic ribonuclease
17. The structure of cytidilyl (2′,5′) adenosine when bound to pancreatic ribonuclease S
18. The structures of RNase A complexed with 3′-CMP and d(CpA): Active site conformation and conserved water molecules
19. Novel nonproductively bound ribonuclease inhibitor complexes. High resolution X-ray refinement studies on the binding of RNase A to cytidylyl-2′,5′-guanosine (2′,5′CpG) and deoxycytidylyl-3′,5′-guanosine (3′,5′dCpdG)
20. A new remote subsite in ribonuclease A
21. Structural determinants of enzymatic processivity
22. Excavating an active site: The nucleobase specificity of ribonuclease A
23. A residue to residue hydrogen bond mediates the nucleotide specificity of ribonuclease A
24. Role of Phe 120 in the activity and structure of bovine pancreatic ribonuclease A
25. Structural and functional changes in bovine pancreatic ribonuclease A by the replacement of Phe 120 with other hydrophobic residues
26. Active site of RNase: Neutron diffraction study of a complex with uridine vanadate, a transition-state analog
27. Identification by site-directed mutagenesis of amino acids in the B2 subsite of bovine pancreatic ribonuclease A
28. The role of non-catalytic binding subsites in the endonuclease activity of bovine pancreatic ribonuclease A
29. Relation between structure and function in some partially synthetic ribonuclease S′. II. Kinetic determinations on (Orn10, Glu11),(Orn10, Leu11)- and (Orn10, Lys11)-RNase S′
30. Reverse transphosphorylation by ribonuclease A needs an intact P2-binding site. Point mutations at Lys7 and Arg10 alter the catalytic properties of the enzyme
31. Coulombic forces in protein-RNA interactions: Binding and cleavage by ribonuclease A and variants at Lys7, Arg10, and Lys66
32. His ... Asp catalytic dyad of ribonuclease A: Structure and function of the wild type, D121N, and D121A enzymes
33. Coulombic effects on remote subsites on the active site of ribonuclease A
34. Aspartic acid-121 functions at the active site of bovine pancreatic ribonuclease
35. a shifts accompanying the inactivating Asp121-Asn substitution in a semisynthetic bovine pancreatic ribonuclease
36. Structural changes that accompany the reduced catalytic efficiency of two semisynthetic ribonuclease analogs
37. a values in the wild-type, D121N, and D121A enzymes
38. His ... Asp catalytic dyad of ribonuclease A: Conformational stability of the wild-type, D121N, D 121A, and H119A enzymes
39. Contribution of a tyrosine side chain to ribonuclease A catalysis and stability
40. Contribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease A
41. Structural characterization of an analog of the major rate-determining disulfide folding intermediate of bovine pancreatic ribonuclease A
42. 15N resonance assignments for wild-type and [C65S, C72S] mutant forms
43. Synthesis of peptide analogs of the N-terminal eicosapeptide sequence of ribonuclease A. VII. Synthesis of Ile8, Orn10- and Ala 8, Orn10eicosapeptides
44. Kinetic and conformational studies on some partially synthetic ribonuclease S′ analogues modified in position 8
45. Mechanism of reductive protein unfolding
46. Nonrandom distribution of the one-disulfide intermediates in the regeneration of ribonuclease A
47. Regeneration of bovine pancreatic ribonuclease A: Identification of two nativelike three-disulfide intermediates involved in separate pathways
48. Regeneration of bovine pancreatic ribonuclease A: Detailed kinetic analysis of two independent folding pathways
49. Distribution of disulfide bonds in the two-difulfide intermediates in the regeneration of bovine pancreatic ribonuclease A: Further insights into the folding process
50. Kinetic and thermodynamic studies of the folding/unfolding of a tryptophan-containing mutant of ribonuclease A
51. Proline isomerization in unfolded ribonuclease A. The equilibrium between fast-folding and slow-folding species is independent of temperature
52. Folding pathway of guanidine-denatured disulfide-intact wild type and mutant bovine pancreatic ribonuclease A
53. A very fast phase in the refolding of disulfide-intact ribonuclease A: Implication for the refolding and unfolding pathways
54. The nature of the initial step in the conformational folding of disulfide-intact ribonuclease A
55. Circular dichroism evidence for the presence of burst-phase intermediates on the conformational folding pathway of ribonuclease A
56. Structure of a hydrophobically collapsed intermediate on the conformational folding pathway of ribonuclease A probed by hydrogendeutrium exchange
57. Nature of the early folding intermediate of ribonuclease A.
58. Regeneration studies of an analog of ribonuclease A missing disulfide bonds 65-72 and 40- 95
59. Regeneration of three-disulfide mutants of bovine pancreatic ribonuclease A missing the 65-72 disulfide bond: Characterization of a minor folding pathway of ribonuclease A and kinetic roles of Cys 65 and Cys72
60. Folding and unfolding kinetics of the proline-to-alanine mutants of bovine pancreatic ribonuclease A
61. Proline isomerization in bovine pancreatic ribonuclease A. I. Unfolding conditions
62. Conformational unfolding studies of three-disulfide mutants of bovine pancreatic ribonuclease A and the coupling of proline isomerization to disulfide redox reactions
63. Kinetic folding of a three-disulfide mutant of bovine pancreatic ribonuclease A missing the [40-95] disulfide bond
64. Structural characterization of a three-disulfide intermediate of ribonuclease A involved in both the folding and unfolding pathways
65. The preparation of subtilisin-modified ribonuclease and the separation of the peptide and protein components
66. A helix stop signal in the isolated S-peptide of ribonuclease A
67. 1H-NMR data
68. On the fundamental role of the Glu2- ... Arg10+ salt bridge in the folding of isolated ribonuclease A S-peptide
69. Immunological determination of the order of folding of proteins of the molecule during air oxidation of reduced ribonuclease
70. The influence of amino acid side-chains on α-helix stability: S-peptide analogues and related ribonuclease S′
71. +
72. Structure of phosphate-free ribonuclease A refined at 1.26 Å
73. Tyrosyl interactions in the folding and unfolding of bovine pancreatic ribonuclease A: A study of tyrosine-to-phenylalanine mutants
74. Structure and stability of the P 93G variant of ribonuclease A
75. The structural roles of amino acid residues near the carboxyl terminus of bovine pancreatic ribonuclease A
76. Reactivation of des(119-, 120-, or 121-124) ribonuclease A by mixture with synthetic COOH-terminal peptide of varying length
77. Formation of randomly paired disulfide bonds in des-(121-124)-ribonuclease after reduction and reoxidation
78. Preparation of pancreatic ribonuc lease 1-114 and 1-115 and their reactivation by mixture with synthetic COOH-terminal peptides
79. Effect of mutagenic replacement of the carboxyl terminal amino acid, Val 124, on the properties and regeneration of bovine pancreatic ribonuclease A
80. Primary structure effects on peptide group hydrogen exchange
81. Early steps in the refolding reaction of reduced ribonuclease A
82. The burst phase in ribonuclease A folding and solvent dependence of the unfolded state
83. Intrinsic stabilities of portions of the ribonuclease molecule
84. Location of the antigenic determinants of bovine pancreatic ribonuclease
85. Speeding along the protein folding highway, are we reading the signs correctly?
86. Distribution of intramolecular distances in the reduced and denatured states of bovine pancreatic ribonuclease A. Folding initiation structures in the C-terminal portions of the reduced protein
87. Solution conformations and thermodynamics of structured peptides: Molecular dynamics simulation with an implicit solvation model
88. A possible folding pathway of bovine pancreatic RNase
89. Prediction of protein conformation
90. Study of RNase A mechanism and folding by means of synthetic 63-residue analogs
91. Predicting the protein folding nucleus from a sequence
92. 1H-NMR assignment and folding of the isolated ribonuclease 21- 42 fragment
93. 1H NMR and CD evidence of the folding of the isolated ribonuclease 50- 61 fragment
94. Local structure in a tryptic fragment of performic acid oxidized ribonuclease A corresponding to a proposed polypeptide chain-folding initiation site detected by tyrosine fluorescence lifetime and proton magnetic resonance measurements
95. Conformational studies of a peptide corresponding to a region of the C-terminus of ribonuclease A: Implications as a potential chain-folding initiation site
96. Energetic and structural basis for the preferential formation of the native disulfide loop involving Cys 65 and Cys72 in synthetic peptide fragments derived from the sequence of ribonuclease A
97. Thermodynamic analysis of the effect of selective monodeamidation at asparagine 67 in ribonuclease A
98. Selective deamidation of ribonuclease A. Isolation and characterization of the resulting isoaspartyl and aspartyl derivatives
99. Deamidation in proteins: The crystal structure of bovine pancreatic ribonuclease with an isoaspartyl residue at position 67
100. Valine 108, a chain-folding initiation site-belonging residue, crucial for the ribonuclease A stability
101. Pressure versus heat-induced unfolding of ribonuclease A: The case of hydrophobic interactions within a chain-folding initiation site
102. Pressure versus temperature unfolding of ribonuclease A: An FTIR spectroscopic characterization of 10 variants at the carboxy-terminal site
103. Comparison of local and global stability of an analogue of a disulfide-folding intermediate with those of the wild-type proteins in bovine pancreatic ribonuclease A: Identification of specific regions of stable structure along the oxidative folding pathway
104. Effects of glycosylation on protein structure and dynamics in ribonuclease B and some of its individual glycoforms
105. Glycoforms modify the dynamic stability and functional activity of an enzyme
106. Kinetic and thermodynamic thermal stabilities of ribonuclease A and ribonuclease B
107. The mechanism of folding of pancreatic ribonuclease is independent of the presence of covalently linked carbohydrate
108. A chaperone-like function of intramolecular high-mannose chains in the oxidative refolding of bovine pancreatic RNase B
109. Protein surface oligosaccharides and protein function
110. Crystalline ribonuclease A loses function below the dynamical transition at 220 K
111. Evidence on the existence of a purine ligand induced conformational change in the active site of bovine pancreatic ribonuclease A studied by proton nuclear magnetic resonance spectroscopy