Role of backbone dynamics and structure in controlling the hydrolysis constants
of serine proteinase inhibitors

The inhibitor is reactive site hydrolyzed (the protein is composed of two
chains since peptide bond between Leu18 and Glu19 is disrupted, the two chains
are connected by disulfide bonds).

Protein inhibitors of serine proteinases: role of backbone structure and dynamics in controlling the hydrolysis constant.

Ovomucoid Third Domain from Indian Peafowl

Crystal And Molecular Structures Of The Complex Of Alpha- Chymotrypsin With Its Inhibitor Turkey Ovomucoid Third Domain At 1.8 Angstroms Resolution

Solution Structure Of Ovomucoid (Third Domain) From Domestic Turkey (298k, Ph 4.1) (Nmr, 50 Structures) (Standard Noesy Analysis)

Solution Structure Of Ovomucoid (Third Domain) From Domestic Turkey (298k, Ph 4.1) (Nmr, 50 Structures) (Refined Model Using Network Editing Analysis)

Crystallographic Refinement Of Japanese Quail Ovomucoid, A Kazal-Type Inhibitor, And Model Building Studies Of Complexes With Serine Proteases

X-Ray Crystal Structure Of The Complex Of Human Leukocyte Elastase (Pmn Elastase) And The Third Domain Of The Turkey Ovomucoid Inhibitor

Solution Structure Of Turkey Ovomucoid Third Domain As Determined From Nuclear Magnetic Resonance Data

Solution Structure Of Reactive-Site Hydrolyzed Turkey Ovomucoid Third Domain By Nuclear Magnetic Resonance And Distance Geometry Methods

Crystal Structure Of The Subtilisin Carlsberg:omtky3 Complex

Refined X-Ray Crystal Structures Of The Reactive Site Modified Ovomucoid Inhibitor Third Domains From Silver Pheasant (Omsvp3(Asterisk)) And From Japanese Quail (Omjpq3(Asterisk))

Structure Of The Complex Of Streptomyces Griseus Protease B And The Third Domain Of The Turkey Ovomucoid Inhibitor At 1.8 Angstroms Resolution

Reactive site hydrolyzed OMTKY3 at pH 6.0 and pH 3.9 and 298K