1hym: Difference between revisions

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[[Image:1hym.gif|left|200px]]<br /><applet load="1hym" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1hym.gif|left|200px]]<br /><applet load="1hym" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1hym" />

'''HYDROLYZED TRYPSIN INHIBITOR (CMTI-V, MINIMIZED AVERAGE NMR STRUCTURE)'''<br />

==Overview==

Reactive-site (Lys44-Asp45 peptide bond) hydrolyzed Cucurbita maxima, trypsin inhibitor-V (CMTI-V*) was prepared and characterized: In, comparison to the intact form, CMTI-V* exhibited markedly reduced, inhibitory properties and binding affinities toward trypsin and human, blood coagulation factor XIIa. The equilibrium constant of, trypsin-catalyzed hydrolysis, Khyd, defined as [CMTI-V*]/[CMTI-V], was, measured to be approximately 9.4 at 25 degrees C (delta G degrees = -1.3, kcal.mol-1). From the temperature dependence of delta G degrees, the, following thermodynamic parameters were estimated: delta H degrees = 1.6, kcal.mol-1 and delta S degrees = 9.8 eu. In order to understand the, functional and thermodynamic differences between the two forms, the, three-dimensional solution structure of CMTI-V* was determined by a, combined approach of NMR, distance geometry, and simulated annealing, methods. Thus, following sequence-specific and stereospecific resonance, assignments, including those of beta-, gamma-, delta-, and, epsilon-hydrogens and valine methyl hydrogens, 809 interhydrogen distances, and 123 dihedral angle constraints were determined, resulting in the, computation and energy-minimization of 20 structures for CMTI-V*. The, average root mean squared deviation in position for equivalent atoms, between the 20 individual structures and the mean structure obtained by, averaging their coordinates is 0.67 +/- 0.15 A for the main chain atoms, and 1.19 +/- 0.23 A for all the non-hydrogen atoms of residues 5-40 and, residues 48-67.(ABSTRACT TRUNCATED AT 250 WORDS)

Reactive-site (Lys44-Asp45 peptide bond) hydrolyzed Cucurbita maxima trypsin inhibitor-V (CMTI-V*) was prepared and characterized: In comparison to the intact form, CMTI-V* exhibited markedly reduced inhibitory properties and binding affinities toward trypsin and human blood coagulation factor XIIa. The equilibrium constant of trypsin-catalyzed hydrolysis, Khyd, defined as [CMTI-V*]/[CMTI-V], was measured to be approximately 9.4 at 25 degrees C (delta G degrees = -1.3 kcal.mol-1). From the temperature dependence of delta G degrees, the following thermodynamic parameters were estimated: delta H degrees = 1.6 kcal.mol-1 and delta S degrees = 9.8 eu. In order to understand the functional and thermodynamic differences between the two forms, the three-dimensional solution structure of CMTI-V* was determined by a combined approach of NMR, distance geometry, and simulated annealing methods. Thus, following sequence-specific and stereospecific resonance assignments, including those of beta-, gamma-, delta-, and epsilon-hydrogens and valine methyl hydrogens, 809 interhydrogen distances and 123 dihedral angle constraints were determined, resulting in the computation and energy-minimization of 20 structures for CMTI-V*. The average root mean squared deviation in position for equivalent atoms between the 20 individual structures and the mean structure obtained by averaging their coordinates is 0.67 +/- 0.15 A for the main chain atoms and 1.19 +/- 0.23 A for all the non-hydrogen atoms of residues 5-40 and residues 48-67.(ABSTRACT TRUNCATED AT 250 WORDS)

==About this Structure==

1HYM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Cucurbita_maxima Cucurbita maxima] with ACE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1HYM OCA].

1HYM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Cucurbita_maxima Cucurbita maxima] with <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HYM OCA].

==Reference==

Line 20:

[[Category: hydrolase (serine proteinase)]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 16~~:54:~~55 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:12 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1hym.gif|left|200px]]<br /><applet load="1hym" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1hym.gif|left|200px]]<br /><applet load="1hym" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1hym" />
 '''HYDROLYZED TRYPSIN INHIBITOR (CMTI-V, MINIMIZED AVERAGE NMR STRUCTURE)'''<br />
 ==Overview==
-Reactive-site (Lys44-Asp45 peptide bond) hydrolyzed Cucurbita maxima, trypsin inhibitor-V (CMTI-V*) was prepared and characterized: In, comparison to the intact form, CMTI-V* exhibited markedly reduced, inhibitory properties and binding affinities toward trypsin and human, blood coagulation factor XIIa. The equilibrium constant of, trypsin-catalyzed hydrolysis, Khyd, defined as [CMTI-V*]/[CMTI-V], was, measured to be approximately 9.4 at 25 degrees C (delta G degrees = -1.3, kcal.mol-1). From the temperature dependence of delta G degrees, the, following thermodynamic parameters were estimated: delta H degrees = 1.6, kcal.mol-1 and delta S degrees = 9.8 eu. In order to understand the, functional and thermodynamic differences between the two forms, the, three-dimensional solution structure of CMTI-V* was determined by a, combined approach of NMR, distance geometry, and simulated annealing, methods. Thus, following sequence-specific and stereospecific resonance, assignments, including those of beta-, gamma-, delta-, and, epsilon-hydrogens and valine methyl hydrogens, 809 interhydrogen distances, and 123 dihedral angle constraints were determined, resulting in the, computation and energy-minimization of 20 structures for CMTI-V*. The, average root mean squared deviation in position for equivalent atoms, between the 20 individual structures and the mean structure obtained by, averaging their coordinates is 0.67 +/- 0.15 A for the main chain atoms, and 1.19 +/- 0.23 A for all the non-hydrogen atoms of residues 5-40 and, residues 48-67.(ABSTRACT TRUNCATED AT 250 WORDS)
+Reactive-site (Lys44-Asp45 peptide bond) hydrolyzed Cucurbita maxima trypsin inhibitor-V (CMTI-V*) was prepared and characterized: In comparison to the intact form, CMTI-V* exhibited markedly reduced inhibitory properties and binding affinities toward trypsin and human blood coagulation factor XIIa. The equilibrium constant of trypsin-catalyzed hydrolysis, Khyd, defined as [CMTI-V*]/[CMTI-V], was measured to be approximately 9.4 at 25 degrees C (delta G degrees = -1.3 kcal.mol-1). From the temperature dependence of delta G degrees, the following thermodynamic parameters were estimated: delta H degrees = 1.6 kcal.mol-1 and delta S degrees = 9.8 eu. In order to understand the functional and thermodynamic differences between the two forms, the three-dimensional solution structure of CMTI-V* was determined by a combined approach of NMR, distance geometry, and simulated annealing methods. Thus, following sequence-specific and stereospecific resonance assignments, including those of beta-, gamma-, delta-, and epsilon-hydrogens and valine methyl hydrogens, 809 interhydrogen distances and 123 dihedral angle constraints were determined, resulting in the computation and energy-minimization of 20 structures for CMTI-V*. The average root mean squared deviation in position for equivalent atoms between the 20 individual structures and the mean structure obtained by averaging their coordinates is 0.67 +/- 0.15 A for the main chain atoms and 1.19 +/- 0.23 A for all the non-hydrogen atoms of residues 5-40 and residues 48-67.(ABSTRACT TRUNCATED AT 250 WORDS)
 ==About this Structure==
-HYM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Cucurbita_maxima Cucurbita maxima] with ACE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HYM OCA].
+HYM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Cucurbita_maxima Cucurbita maxima] with <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HYM OCA].
 ==Reference==
@@ Line 20: / Line 20: @@
 [[Category: hydrolase (serine proteinase)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:54:55 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:12 2008''