Studies by 1H nuclear magnetic resonance and distance geometry of the solution conformation of the α-amylase inhibitor Tendamistat

Kline, Allen D.; Braun, Werner; Wüthrich, Kurt

doi:10.1016/0022-2836(86)90519-x

Cited by 174 publications

(64 citation statements)

References 20 publications

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“…The tripeptide Trpi8-Argi()-Tyr2o is assumed to play a major role in the binding to a-amylase. The determination of the solution structure (Kline et al 1986(Kline et al , 1988) yielded a well defined conformation for the complete backbone with the exception of about five residues at the N-terminus and of the C-terminal residue. This structure was based on 842 distance constraints from NOEs and about 70 constraints on dihedral angles.…”

Section: A-amylase Inhibitor (Tendamistat)mentioning

confidence: 99%

Comparison of protein structures determined by NMR in solution and by X-ray diffraction in single crystals

Billeter¹

1992

Quart. Rev. Biophys.

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Following the first determinations of protein structures in the late 1950s and the early 1960s (see for example Kendrewet al.1960; Perutz, 1964), the three-dimensional structures of several hundred proteins have been elucidated by X-ray diffraction on single crystals. By the end of 1991, approximately 150 entries of proteins with substantially different sequences and a well resolved structure (Hobohmet al.1992) were deposited in the Protein Data Bank (Bernsteinet al.1977; Abolaet al.1987). In addition, many structures of homologous proteins or of mutants have been described, bringing the total number of entries to about 600. While it was soon accepted that almost all of these structures do indeed give a correct picture of the fold of the active protein in spite of the non-physiological environment of single crystals, it is not clear to what extent structural details are reliably described by these structures. In particular the surface of a protein may be modified due to the dense packing of protein molecules in the crystal lattice. A detailed knowledge of the protein surface is, however, essential for the understanding of the function of the protein.

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Section: A-amylase Inhibitor (Tendamistat)mentioning

confidence: 99%

Comparison of protein structures determined by NMR in solution and by X-ray diffraction in single crystals

Billeter¹

1992

Quart. Rev. Biophys.

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“…In the case of the a-amylase inhibitor (Kline et al 1986) there are about 500 distance constraints from NMR data. These constraints are to be complemented with about 1500 constraints for bond lengths and bond-angle constraints.…”

Section: Metric Matrix Methodsmentioning

confidence: 99%

“…Having these tools and a good set of distance constraints, it actually could be shown that the hope was justified. A clear test for this hypothesis was presented in the structural determination of the X-ray single crystal and the NMR structure of a-amylase inhibitor where for the first time an independent structural analysis of an unknown structure of a globular protein by both methods was done (Pfiugrath et al 1986;Kline et al 1986). …”

Section: Formulation Of the Mathematical Problemmentioning

confidence: 99%

“…The uniform averaging model (see Section 2.1) proposed in this work was an attempt to include effects of the internal flexibility of the molecule. The partial success of a detailed atomic structure determination of this molecule from a set of semiquantitative NOE measurements and the existence of a computer program to generate structures from the experimental NOE data stimulated improvements in recording NOESY spectra and motivated the collection of rather large distance constraints data sets of proteins (Arseniev et al 1984;Zuiderweg et al 1984;Williamson et al 1985;Braun et al 1986;Kline et al 1986;Wagner et al 1986). …”

Section: Micelle-bound Glucagonmentioning

confidence: 99%

“…This should provide an objective test for the reliability of the NMR structure determination and to make sure that differences and similarities between NMR and X-ray structures are not biased by the exchange of structural information between the two groups using the two different methods. In the future (Braun, 1983) of one of the four NMR structures of a-amylase inhibitor Tendamistat (Kline et al 1986). For each C"-C" atom pair with residue numbers i andj a plus or minus sign is plotted according to the handedness of the two tangent vectors to the polypeptide chain fold at residues »' and./ and the vector connecting residues i and j if the C-C* distance is less than 10 A.…”

Section: A-amylase Inhibitormentioning

confidence: 99%

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Distance geometry and related methods for protein structure determination from NMR data

Braun

1987

Quart. Rev. Biophys.

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212

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The method of choice to reveal the conformation of protein molecules in atomic detail has been X-ray single-crystal analysis. Since the first structural analysis of diffraction patterns, computer calculations have been an important tool in these studies (Blundell & Johnson, 1976). As is described by Sheldrick (1985), it has been taken for granted that a necessary first step in the determination of a protein structure would be writing computer programs to fit structure factors. In contrast the combined use of the structural analysis of NMR data and computer calculations has been quite limited. An early attempt of such structural calculations was the quantitative determination of mononucleotide conformations in solution using lanthanide ion shifts (Barry et al. 1971).

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The Development of NMR

Becker

Fisk

Khetrapal

2007

Encyclopedia of Magnetic Resonance

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Studies by 1H nuclear magnetic resonance and distance geometry of the solution conformation of the α-amylase inhibitor Tendamistat

Cited by 174 publications

References 20 publications

Comparison of protein structures determined by NMR in solution and by X-ray diffraction in single crystals

Comparison of protein structures determined by NMR in solution and by X-ray diffraction in single crystals

Distance geometry and related methods for protein structure determination from NMR data

The Development of NMR

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