✦ LIBER ✦

Structure, strain, and reorganization energy of blue copper models in the protein

✍ Scribed by Ulf Ryde; Mats H. M. Olsson

Publisher: John Wiley and Sons
Year: 2001
Tongue: English
Weight: 247 KB
Volume: 81
Category: Article
ISSN: 0020-7608
DOI: 10.1002/1097-461x(2001)81:5<335::aid-qua1003>3.0.co;2-q

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Protein strain in blue copper proteins s

Protein strain in blue copper proteins studied by free energy perturbations

✍ Jan O.A. De Kerpel; Ulf Ryde 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 306 KB 👁 1 views

Free energy perturbations have been performed on two blue copper proteins, plastocyanin and nitrite reductase. By changing the copper coordination geometry, force constants, and charges, we have estimated the maximum energy with which the proteins may distort the copper coordination sphere. By compa

Challenges in structure prediction of ol

Challenges in structure prediction of oligomeric proteins at the united-residue level: Searching the multiple-chain energy landscape with CSA and CFMC

✍ Jeffrey A. Saunders; Harold A. Scheraga 📂 Article 📅 2003 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 250 KB

13C- and 57Fe-NMR studies of the FeCO un

13C- and 57Fe-NMR studies of the FeCO unit of heme proteins and synthetic model compounds in solution: Comparison with IR vibrational frequencies and X-ray structural data

✍ Charalampos G. Kalodimos; Ioannis P. Gerothanassis; Geoffrey E. Hawkes 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 281 KB 👁 2 views

13C- and 57Fe-NMR spectra of several carbon monoxide hemoprotein models with varying polar and steric effects of the distal organic superstructure, constraints of the proximal side, and solvent polarity are reported. The 13C shieldings of heme models cover a 4.0 ppm range that is extended to 7.0 ppm