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Journal Abstract Search
201 related items for PubMed ID: 9753430
1. The 0.78 A structure of a serine protease: Bacillus lentus subtilisin. Kuhn P, Knapp M, Soltis SM, Ganshaw G, Thoene M, Bott R. Biochemistry; 1998 Sep 29; 37(39):13446-52. PubMed ID: 9753430 [Abstract] [Full Text] [Related]
2. Structure of a serine protease proteinase K from Tritirachium album limber at 0.98 A resolution. Betzel C, Gourinath S, Kumar P, Kaur P, Perbandt M, Eschenburg S, Singh TP. Biochemistry; 2001 Mar 13; 40(10):3080-8. PubMed ID: 11258922 [Abstract] [Full Text] [Related]
7. The influence of solvation on short strong hydrogen bonds: a density functional theory study of the Asp-His interaction in subtilisins. Schiott B. Chem Commun (Camb); 2004 Mar 07; (5):498-9. PubMed ID: 14973576 [Abstract] [Full Text] [Related]
9. Subangstrom crystallography reveals that short ionic hydrogen bonds, and not a His-Asp low-barrier hydrogen bond, stabilize the transition state in serine protease catalysis. Fuhrmann CN, Daugherty MD, Agard DA. J Am Chem Soc; 2006 Jul 19; 128(28):9086-102. PubMed ID: 16834383 [Abstract] [Full Text] [Related]
18. Do enzymes change the nature of transition states? Mapping the transition state for general acid-base catalysis of a serine protease. Bott RR, Chan G, Domingo B, Ganshaw G, Hsia CY, Knapp M, Murray CJ. Biochemistry; 2003 Sep 16; 42(36):10545-53. PubMed ID: 12962477 [Abstract] [Full Text] [Related]
19. Combined high-resolution neutron and X-ray analysis of inhibited elastase confirms the active-site oxyanion hole but rules against a low-barrier hydrogen bond. Tamada T, Kinoshita T, Kurihara K, Adachi M, Ohhara T, Imai K, Kuroki R, Tada T. J Am Chem Soc; 2009 Aug 12; 131(31):11033-40. PubMed ID: 19603802 [Abstract] [Full Text] [Related]