Whitlow M - Search Results

1

Nuclear magnetic resonance study of the solution structure of alpha 1-purothionin. Sequential resonance assignment, secondary structure and low resolution tertiary structure.

Clore GM, Sukumaran DK, Gronenborn AM, Teeter MM, Whitlow M, Jones BL. Clore GM, et al. Among authors: whitlow m. J Mol Biol. 1987 Feb 5;193(3):571-8. doi: 10.1016/0022-2836(87)90267-1. J Mol Biol. 1987. PMID: 3586031

2

Energy minimization for tertiary structure prediction of homologous proteins: alpha 1-purothionin and viscotoxin A3 models from crambin.

Whitlow M, Teeter MM. Whitlow M, et al. J Biomol Struct Dyn. 1985 Feb;2(4):831-48. doi: 10.1080/07391102.1985.10506327. J Biomol Struct Dyn. 1985. PMID: 3917120

3

Crystal structure of a protein-toxin alpha 1-purothionin at 2.5A and a comparison with predicted models.

Teeter MM, Ma XQ, Rao U, Whitlow M. Teeter MM, et al. Among authors: whitlow m. Proteins. 1990;8(2):118-32. doi: 10.1002/prot.340080203. Proteins. 1990. PMID: 2235992

4

Test of circular dichroism (CD) methods for crambin and CD-assisted secondary structure prediction of its homologous toxins.

Teeter MM, Whitlow M. Teeter MM, et al. Among authors: whitlow m. Proteins. 1988;4(4):262-73. doi: 10.1002/prot.340040405. Proteins. 1988. PMID: 3253736

5

1.67-A X-ray structure of the B2 immunoglobulin-binding domain of streptococcal protein G and comparison to the NMR structure of the B1 domain.

Achari A, Hale SP, Howard AJ, Clore GM, Gronenborn AM, Hardman KD, Whitlow M. Achari A, et al. Among authors: whitlow m. Biochemistry. 1992 Nov 3;31(43):10449-57. doi: 10.1021/bi00158a006. Biochemistry. 1992. PMID: 1420164

6

A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G.

Gronenborn AM, Filpula DR, Essig NZ, Achari A, Whitlow M, Wingfield PT, Clore GM. Gronenborn AM, et al. Among authors: whitlow m. Science. 1991 Aug 9;253(5020):657-61. doi: 10.1126/science.1871600. Science. 1991. PMID: 1871600

7

A-DNA accommodates adducts derived from diol epoxides of polycyclic aromatic hydrocarbons bound in a "side-stacking" mode.

Andersen RW, Whitlow MD, Teeter MM, Mohr SC. Andersen RW, et al. Among authors: whitlow md. J Biomol Struct Dyn. 1987 Oct;5(2):383-404. doi: 10.1080/07391102.1987.10506401. J Biomol Struct Dyn. 1987. PMID: 3152156

8

Mapping the binding site of aflatoxin B1 in DNA: molecular modeling of the binding sites for the N(7)-guanine adduct of aflatoxin B1 in different DNA sequences.

Loechler EL, Teeter MM, Whitlow MD. Loechler EL, et al. Among authors: whitlow md. J Biomol Struct Dyn. 1988 Jun;5(6):1237-57. doi: 10.1080/07391102.1988.10506467. J Biomol Struct Dyn. 1988. PMID: 3152159

As the sequence is changed, one particular external binding site would be expected to give a pattern of reactivities that is reasonably consistent with the observed sequence specificity of binding that AFB1 shows in its reaction with DNA (Benasutti, M., Ejadi, S., Whitl …

As the sequence is changed, one particular external binding site would be expected to give a pattern of reactivities that is reasonably cons …

9

Structure of human plasminogen kringle 4 at 1.68 a and 277 K. A possible structural role of disordered residues.

Stec B, Yamano A, Whitlow M, Teeter MM. Stec B, et al. Among authors: whitlow m. Acta Crystallogr D Biol Crystallogr. 1997 Mar 1;53(Pt 2):169-78. doi: 10.1107/S0907444996012267. Acta Crystallogr D Biol Crystallogr. 1997. PMID: 15299951

10

Crystallization of single-chain Fv proteins.

Essig NZ, Wood JF, Howard AJ, Raag R, Whitlow M. Essig NZ, et al. Among authors: whitlow m. J Mol Biol. 1993 Dec 5;234(3):897-901. doi: 10.1006/jmbi.1993.1638. J Mol Biol. 1993. PMID: 8254684

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