about
The formation and stabilization of protein structureNucleation, rapid folding, and globular intrachain regions in proteinsBovine pancreatic ribonuclease: fifty years of the first enzymatic reaction mechanismThe influence of short-range interactions on protein onformation. II. A model for predicting the alpha-helical regions of proteinsStudying and polishing the PDB's macromoleculesHelix probability profiles of denatured proteins and their correlation with native structuresA brief history of macromolecular crystallography, illustrated by a family tree and its Nobel fruitsThe crystal structure of recombinant rat pancreatic RNase AA new crystal form of bovine pancreatic RNase A in complex with 2′-deoxyguanosine-5′-monophosphateInteractions of gold-based drugs with proteins: crystal structure of the adduct formed between ribonuclease A and a cytotoxic gold(III) compoundThe 2-A resolution structure of a thermostable ribonuclease A chemically cross-linked between lysine residues 7 and 41The crystal structure of a 3D domain-swapped dimer of RNase A at a 2.1-A resolutionBiophysical highlights from 54 years of macromolecular crystallographyStructural and functional importance of local and global conformational fluctuations in the RNase A superfamily.Revealing structural views of biology.A bait and switch hapten strategy generates catalytic antibodies for phosphodiester hydrolysis.His...Asp catalytic dyad of ribonuclease A: structure and function of the wild-type, D121N, and D121A enzymes.One-Pot Synthesis of Multiple Protein-Encapsulated DNA Flowers and Their Application in Intracellular Protein Delivery.His ... Asp catalytic dyad of ribonuclease A: histidine pKa values in the wild-type, D121N, and D121A enzymesA new basis for interpreting the circular dichroic spectra of proteins.Cancer chemotherapy--ribonucleases to the rescue.Retinol-binding protein: the transport protein for vitamin A in human plasmaCorrelation of amino acid sequence and conformation in tobacco mosaic virus.Both the fast and slow refolding reactions of ribonuclease A yield native enzyme.Squalene and sterol carrier protein: structural properties, lipid-binding, and function in cholesterol biosynthesis.Nuclear magnetic resonance study of the thermal denaturation of ribonuclease A: implications for multistate behavior at low pH.Orientation of histidine residues in RNase A: neutron diffraction study.Unexpected DNA loss mediated by the DNA binding activity of ribonuclease AThe mechanism of rate-limiting motions in enzyme function.Structure and stability of the P93G variant of ribonuclease A.The influence of short-range interactions on protein conformation. 3. Dipeptide distributions in proteins of known sequence and structure.The mechanism of action of ribonucleaseNuclear magnetic resonance studies of the structure and binding sites of enzymes. I. Histidine residues.Minimization of polypeptide energy. II. Preliminary structures of oxytocin, vasopressin, and an octapeptide from ribonuclease.Assignment of the histidine peaks in the nuclear magnetic resonance spectrum of ribonuclease.Nuclear magnetic resonance studies of the structure and binding sites of enzymes. IV. Cytidine 3'-monophosphate binding to ribonuclease.The influence of short-range interactions on protein conformation. I. Side chain-backbone interactions within a single peptide unit.The estimation of protein secondary structure by laser Raman. Spectroscopy from the amide III' intensity distribution.Poly(L-alanine) as a universal reference material for understanding protein energies and structures.F-actin is intermolecularly crosslinked by N,N'-p-phenylenedimaleimide through lysine-191 and cysteine-374.
P2860
Q24530561-7523462F-0E5C-452A-AC42-4D7C36F9F81BQ24564344-55488951-CE76-44C5-9D13-34522B801995Q24595662-65782EF1-5D48-44A5-A3CC-2FD74E7ED250Q24632800-B00384B5-F2F4-4709-A68D-483C71B9A421Q24634083-3E4CE518-B3FB-4BE8-9A19-9BDB1ADE5BF3Q24634691-C41C9C2C-5034-4D27-B47F-72AA930F4849Q26823889-79DD2AC5-6859-4C5C-B1B3-ABFF06F6B84BQ27617726-C0161320-001C-4C76-B4D1-6E4B149D8A23Q27647797-377ED37E-F31E-487D-A471-14EC5A1DD560Q27687736-F5FDF113-DE2B-4BD8-A93F-2DD43264EE40Q27728968-119F3A25-89A4-4FE8-84A5-ADA3E1B90966Q27748984-FE539343-B5EE-48C0-9EA5-82B7346C1598Q28658133-6B93287A-941D-4236-9498-1243A1CBE19DQ30431892-B992E037-1A4B-4905-8B3E-DEC59233647DQ30432666-E8C1F60A-89B3-46BB-B8AF-B4FB7150A59FQ32062852-CBCE407A-391A-4DEC-8C8B-90468E8B68B5Q33771406-887624BD-F53D-4484-AA45-C1DB43FB817FQ33917951-398247EF-163D-4EBE-9E86-8E5BCD12C83AQ34170031-5CA49457-3A1B-4F92-A754-70E04A9A10DAQ34230455-0FAE3536-8660-42A6-AC2B-316EBB3B3734Q34254671-0C5BCA9F-182D-4780-B903-2C0B2D4951DDQ34278411-E3249CBC-7227-4EEE-95FC-A646B6A82CFFQ34354402-15336224-5145-464C-9C7B-B540D3BC0371Q34744684-7324D48C-9199-4EE9-BE13-AAB8BA5F08C0Q35094359-9630B159-4277-41CE-A8CA-10C5FA4142F5Q35099550-31296521-55A6-4A75-B1CE-84A1FB980977Q35359902-BAE90C89-915E-4F9F-A215-22EF3D5F510AQ35515684-8F72B03B-A825-48EA-8057-2A06616EEDFEQ35901179-D807DDFA-0C66-41D8-AF4B-2F881D9B5178Q36281098-C630ECF4-71F0-4DD7-B96D-4543B344E90EQ36448242-ED44774B-C967-4900-86A6-8C051A6F6F01Q36450024-7E080089-B21B-463D-8F00-D1EA94855712Q36454713-5F2C81AC-17C4-4BDB-BC3E-29A6CE5CDF52Q36454805-D543BC0E-6B7A-4689-93D4-67318BA71CC4Q36475095-4C27BC2E-8BD7-48C7-AAD0-FCD6B5504159Q36475541-A95E2489-E040-43D7-9ACD-3AA2E2AB1FD3Q36475943-514177C5-9C17-4DDC-8F7F-9D76F7A5A19AQ36595021-C5248814-3061-4BD6-B3CB-F603FEDA7302Q37326687-A4056F37-B314-44E1-B509-CD8563F80480Q37574687-22AE8DF7-EF71-48A6-895E-15FC350CCA29
P2860
description
1967 nî lūn-bûn
@nan
1967 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1967 թվականի մարտին հրատարակված գիտական հոդված
@hy
1967年の論文
@ja
1967年論文
@yue
1967年論文
@zh-hant
1967年論文
@zh-hk
1967年論文
@zh-mo
1967年論文
@zh-tw
1967年论文
@wuu
name
Tertiary structure of ribonuclease
@ast
Tertiary structure of ribonuclease
@en
Tertiary structure of ribonuclease
@nl
type
label
Tertiary structure of ribonuclease
@ast
Tertiary structure of ribonuclease
@en
Tertiary structure of ribonuclease
@nl
prefLabel
Tertiary structure of ribonuclease
@ast
Tertiary structure of ribonuclease
@en
Tertiary structure of ribonuclease
@nl
P2093
P356
P1433
P1476
Tertiary structure of ribonuclease
@en
P2093
P2860
P2888
P356
10.1038/213862A0
P407
P577
1967-03-04T00:00:00Z
P6179
1038405748