Two-dimensional NMR studies of squash family inhibitors. Sequence-specific proton assignments and secondary structure of reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor III

Ramaswamy Krishnamoorthi; Yu Xi Gong; Chan Lan Sun Lin; David VanderVelde

doi:10.1021/bi00118a036

Two-dimensional NMR studies of squash family inhibitors. Sequence-specific proton assignments and secondary structure of reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor III

Biochemistry ◽

10.1021/bi00118a036 ◽

1992 ◽

Vol 31 (3) ◽

pp. 898-904 ◽

Cited By ~ 7

Author(s):

Ramaswamy Krishnamoorthi ◽

Yu Xi Gong ◽

Chan Lan Sun Lin ◽

David VanderVelde

Keyword(s):

Secondary Structure ◽

Trypsin Inhibitor ◽

Two Dimensional ◽

Cucurbita Maxima ◽

Reactive Site ◽

Nmr Studies

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NMR studies of internal dynamics of serine proteinase protein inhibitors: Binding region mobilities of intact and reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor (CMTI)-III of the squash family and comparison with those of counterparts of CMTI

Protein Science ◽

10.1002/pro.5560070114 ◽

1998 ◽

Vol 7 (1) ◽

pp. 132-141 ◽

Cited By ~ 10

Author(s):

Jianhua Liu ◽

Yuxi Gong ◽

Om Prakash ◽

Ramaswamy Krishnamoorthi ◽

Lisa Wen ◽

...

Keyword(s):

Trypsin Inhibitor ◽

Serine Proteinase ◽

Cucurbita Maxima ◽

Reactive Site ◽

Binding Region ◽

Protein Inhibitors ◽

Nmr Studies ◽

Internal Dynamics

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Two-dimensional NMR studies of Kazal proteinase inhibitors. 2. Sequence-specific assignments and secondary structure of reactive site modified turkey ovomucoid third domain

Biochemistry ◽

10.1021/bi00407a040 ◽

1988 ◽

Vol 27 (7) ◽

pp. 2529-2539 ◽

Cited By ~ 14

Author(s):

Gyung Ihm Rhyu ◽

John L. Markley

Keyword(s):

Secondary Structure ◽

Proteinase Inhibitors ◽

Two Dimensional ◽

Reactive Site ◽

Nmr Studies ◽

Ovomucoid Third Domain

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Structural consequences of the natural substitution, E9K, on reactive-site-hydrolyzed squash (Cucurbita maxima) trypsin inhibitor (CMTI), as studied by two-dimensional NMR

Biochemistry ◽

10.1021/bi00136a007 ◽

1992 ◽

Vol 31 (21) ◽

pp. 4965-4969 ◽

Cited By ~ 2

Author(s):

Ramaswamy Krishnamoorthi ◽

Chan Lan Sun Lin ◽

David VanderVelde

Keyword(s):

Trypsin Inhibitor ◽

Two Dimensional ◽

Cucurbita Maxima ◽

Reactive Site

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Two-dimensional NMR studies on des-pentapeptide-insulin. Proton resonance assignments and secondary structure analysis

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1990.tb19104.x ◽

1990 ◽

Vol 191 (1) ◽

pp. 147-153 ◽

Cited By ~ 25

Author(s):

Rolf BOELENS ◽

Maria Luisa GANADU ◽

Patricia VERHEYDEN ◽

Robert KAPTEIN

Keyword(s):

Secondary Structure ◽

Structure Analysis ◽

Resonance Assignments ◽

Two Dimensional ◽

Proton Resonance ◽

Nmr Studies ◽

Secondary Structure Analysis

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Two-dimensional 1H-NMR studies of maize lipid-transfer protein. Sequence-specific assignment and secondary structure

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1994.tb18957.x ◽

1994 ◽

Vol 222 (3) ◽

pp. 1047-1054 ◽

Cited By ~ 17

Author(s):

Marie-Christine PETIT ◽

Patrick SODANO ◽

Didier MARION ◽

Marius PTAK

Keyword(s):

Secondary Structure ◽

1H Nmr ◽

Protein Sequence ◽

Lipid Transfer Protein ◽

Two Dimensional ◽

Lipid Transfer ◽

Nmr Studies ◽

Transfer Protein ◽

Sequence Specific Assignment ◽

Specific Assignment

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Natural abundance 15 N NMR assignments delineate structural differences between intact and reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor III

FEBS Letters ◽

10.1016/0014-5793(92)80607-i ◽

1992 ◽

Vol 304 (2-3) ◽

pp. 149-152 ◽

Cited By ~ 1

Author(s):

Ramaswamy Krishnamoorthi ◽

Sylvia Nemmers ◽

Brian Tobias

Keyword(s):

Trypsin Inhibitor ◽

Nmr Assignments ◽

Natural Abundance ◽

Cucurbita Maxima ◽

Reactive Site ◽

Structural Differences

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Reactive-Site Hydrolyzed Cucurbita maxima Trypsin Inhibitor-V: Function, Thermodynamic Stability, and NMR Solution Structure

Biochemistry ◽

10.1021/bi00038a001 ◽

1995 ◽

Vol 34 (38) ◽

pp. 12087-12094 ◽

Cited By ~ 8

Author(s):

Mengli Cai ◽

YuXi Gong ◽

Om Prakash ◽

Ramaswamy Krishnamoorthi

Keyword(s):

Trypsin Inhibitor ◽

Thermodynamic Stability ◽

Solution Structure ◽

Cucurbita Maxima ◽

Reactive Site ◽

Nmr Solution Structure

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Two-dimensional proton NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure

Biochemistry ◽

10.1021/bi00110a024 ◽

1991 ◽

Vol 30 (46) ◽

pp. 11186-11192 ◽

Cited By ~ 12

Author(s):

Hans Robert Kalbitzer ◽

Klaus Peter Neidig ◽

Wolfgang Hengstenberg

Keyword(s):

Staphylococcus Aureus ◽

Secondary Structure ◽

Proton Nmr ◽

Two Dimensional ◽

Nmr Studies

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Two-dimensional NMR studies and secondary structure of cobrotoxin in aqueous solution

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1990.tb19401.x ◽

1990 ◽

Vol 193 (3) ◽

pp. 789-795 ◽

Cited By ~ 14

Author(s):

Chin YU ◽

Chang-Shin LEE ◽

Li-Chin CHUANG ◽

You-Rhon SHEI ◽

Chi Ying WANG

Keyword(s):

Aqueous Solution ◽

Secondary Structure ◽

Two Dimensional ◽

Nmr Studies

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Two-dimensional proton-NMR studies on a hybrid peptide between cecropin A and melittin. Resonance assignments and secondary structure

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1991.tb16122.x ◽

1991 ◽

Vol 199 (2) ◽

pp. 285-291 ◽

Cited By ~ 28

Author(s):

David SIPOS ◽

Kasibhatla CHANDRASEKHAR ◽

Klas ARVIDSSON ◽

Ake ENGSTROM ◽

Anders EHRENBERG

Keyword(s):

Secondary Structure ◽

Proton Nmr ◽

Resonance Assignments ◽

Two Dimensional ◽

Hybrid Peptide ◽

Nmr Studies ◽

Cecropin A

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