| Entry ID |
Data summary |
Entry Title |
Citation Title |
Authors |
| 6160 |
Chemical Shifts: 1 set
|
Structural and biochemical evidence for disulfide bond heterogeneity in active forms of the somatomedin B domain of human vitronectin |
Disulfide Bonding Arrangements in Active Forms of the Somatomedin B Domain of Human Vitronectin
|
A Jagielska, D Loskutoff, G Kroon, H Dyson, H Scheraga, J Neels, M Churchill, P Dawson, R De Guzman, S Curriden, S Oldziej, Y Kamikubo |
| 4032 |
Chemical Shifts: 1 set
|
1H, 13C and 15N Resonance Assignments for the Bovine Pancreatic [C65S, C72S] Ribonuclease A at pH* 4.6 and Temperature of 20 deg. C |
NMR Structural Analysis of an Analog of an Intermediate Formed in the Rate-Determining Step of One Pathway in the Oxidative Folding of Bovine Pancreatic Ribonuclease A: Automated Analysis of 1H, 13C and 15N Resonance Assignments for Wild-Type and [C65S, C72S] Mutant Forms.
|
Carlos B Rios, Diane E Zimmerman, Gaetano T Montelione, Harold A Scheraga, John H Laity, Sakurako Shimotakahara |
| 4031 |
Chemical Shifts: 1 set
|
1H, 13C and 15N Resonance Assignments for the Bovine Pancreatic Ribonuclease A at pH* 4.6 and Temperature of 20 Deg. C |
NMR Structural Analysis of an Analog of an Intermediate Formed in the Rate-Determining Step of One Pathway in the Oxidative Folding of Bovine Pancreatic Ribonuclease A: Automated Analysis of 1H, 13C and 15N Resonance Assignments for Wild-Type and [C65S, C72S] Mutant Forms.
|
Carlos B Rios, Diane E Zimmerman, Gaetano T Montelione, Harold A Scheraga, John H Laity, Sakurako Shimotakahara |
| 385 |
Chemical Shifts: 1 set
|
Proton NMR Assignments and Regular Backbone Structure of Bovine Pancreatic Ribonuclease A in Aqueous Solution |
Proton NMR Assignments and Regular Backbone Structure of Bovine Pancreatic Ribonuclease A in Aqueous Solution
|
Andrew D Robertson, Enrico O Purisima, H A Scheraga, Margaret A Eastman |
| 401 |
Chemical Shifts: 1 set
|
High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen |
High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen
|
Feng Ni, H A Scheraga, Lea Doerr Bullock, Meheryar N Rivetna, Yasuo Konishi |
| 1072 |
Chemical Shifts: 1 set
|
Nonnative Isomers of Proline-93 and -114 Predominate in Heat-Unfolded Ribonuclease A |
Nonnative Isomers of Proline-93 and -114 Predominate in Heat-Unfolded Ribonuclease A
|
H A Scheraga, Marc Adler |
| 417 |
Chemical Shifts: 1 set
|
High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen |
High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen
|
Feng Ni, H A Scheraga, Lea Doerr Bullock, Meheryar N Rivetna, Yasuo Konishi |
| 490 |
Chemical Shifts: 1 set
|
Thrombin-Bound Conformation of the C-Terminal Fragments of Hirudin Determined by Transferred Nuclear Overhauser Effects |
Thrombin-Bound Conformation of the C-Terminal Fragments of Hirudin Determined by Transferred Nuclear Overhauser Effects
|
Feng Ni, H A Scheraga, Yasuo Konishi |
| 402 |
Chemical Shifts: 1 set
|
High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen |
High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen
|
Feng Ni, H A Scheraga, Lea Doerr Bullock, Meheryar N Rivetna, Yasuo Konishi |
| 1674 |
Chemical Shifts: 1 set
|
Sequence-specific 1H-NMR Assignments and Identification of Slowly Exchanging Amide Protons in Murine Epidermal Growth Factor |
Sequence-specific 1H-NMR Assignments and Identification of Slowly Exchanging Amide Protons in Murine Epidermal Growth Factor
|
G T Montelione, H A Scheraga, Kurt Wuthrich |
| 2201 |
Chemical Shifts: 1 set
|
Solution Structure of Murine Epidermal Growth Factor Determined by NMR Spectroscopy and Refined by Energy Minimization with Restraints |
Solution Structure of Murine Epidermal Growth Factor Determined by NMR Spectroscopy and Refined by Energy Minimization with Restraints
|
A W Burgess, E C Nice, Gerhard Wagner, G T Montelione, H A Scheraga, Kenneth D Gibson, Kurt Wuthrich |
