N.m.r. studies of myelin basic protein. Conformation of a peptide that is an antigenic determinant for B-cell reactivity

Mendz, George L.; Moore, Walter J.

doi:10.1042/bj2290305

Cited by 18 publications

(4 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The typical values of 3/nhch obtained in unstructured peptides are about 7-7.5 Hz (Mendz & Moore, 1985) so that a value of 6 Hz may indicate some rotational constraint. Values as low as 5.2 Hz, however, are definite indicators of restricted motion unlike that observed in random coils (De Marco et al, 1978).…”

Section: Discussionmentioning

confidence: 98%

“…coupling technique was used to irradiate the aCH resonances, and the NH resonance collapse was observed in the coupled NH proton. The assignments are listed in Table II together with the 3/Chnh coupling constants and the expected from NH resonances in small unstructured peptides, which exhibit coupling constants of 7-7.5 Hz (Bundi & Wüthrich, 1979;Mendz & Moore, 1985). Several of the coupling constants are small, with values as low as 5.2 Hz, indicating that at least some of the backbone of the peptide is significantly constrained.…”

mentioning

confidence: 99%

See 1 more Smart Citation

NMR of a synthetic peptide spanning the triphosphate binding site of adenosine 5'-triphosphate in actin

Barden¹,

Kemp²

1987

Biochemistry

View full text Add to dashboard Cite

The amino acid residues 114-118 in actin were found to be implicated strongly in the binding of nucleotide, and as would be expected for such an important binding site, they are located in a completely conserved region of the actin sequence. A 19-residue peptide with the actin sequence 106-124 was synthesized in order to span the putative triphosphate binding site. Proton NMR spectra of the actin peptide 114-118 in the presence and absence of ATP indicated that Arg-116 and Lys-118 are particularly involved in binding ATP. A strong binding of ATP to the peptide 106-124 also was measured. Tripolyphosphate bound to the peptide 106-124 somewhat more weakly than ATP. Binding involved residues 115-118 and 121-124, indicating the presence of a reverse turn between these segments. Proton resonances were assigned by using two-dimensional double quantum correlated spectroscopy, one-dimensional spin decoupling techniques, one-dimensional nuclear Overhauser enhancement difference spectroscopy, and pH titration. The alpha CH resonances of Ala-3 and Asn-6 are markedly shifted downfield with respect to values in small unstructured peptides due to their close proximity to the side chains of Pro-4 and Pro-7, respectively. Several other resonances display chemical shifts which are indicative of a structured environment. Assignment of the amide proton resonances in H2O and measurements of the coupling constant 3JHNCH and the chemical shifts of the amide protons reveal that much of the synthetic peptide, particularly the backbone, exhibits a highly structured environment and represents a good model for the triphosphate binding site in actin.

show abstract

Section: Discussionmentioning

confidence: 98%

mentioning

confidence: 99%

NMR of a synthetic peptide spanning the triphosphate binding site of adenosine 5'-triphosphate in actin

Barden¹,

Kemp²

1987

Biochemistry

View full text Add to dashboard Cite

show abstract

“…There is considerable evidence that continuous antigenic sites are often located in or nearby turns of proteins (Mendz and Moore, 1985;Williamson et al, 1986;Laczko et al, 1992). Thus, three turn scales were developed using a threedimensional database of high-resolution proteins extracted from the Brookhaven Protein Data Bank, corresponding to (1) helical turns, (2) hairpin turns and (3) non-specific turns, respectively.…”

Section: Physico-chemical and Structural Scales For Predicting Amino mentioning

confidence: 99%

Recent Developments with B-Cell Epitope Identification for Predictive Studies

Roggen

2006

Journal of Immunotoxicology

View full text Add to dashboard Cite

This review discusses currently available methods for predicting B-cell epitopes on proteins. The use of animals for assessing protein immunogenicity is addressed primarily to highlight the differences in B- and T-cell epitope recognition between species. These differences have to be considered when interpreting potential B-cell epitopes identified by the methods addressed here. "In vitro alternatives" focuses on the strengths and limitations of peptide-based technologies. Three types of computer-based methods for identifying potential B-cell epitopes are discussed: (i) methods applying physico-chemical and structural propensity scales for predicting linear epitopes from the primary structure of a protein, (ii) comparative methods basing prediction upon amino acid sequence and structural similarities between antigenically known and unknown proteins, and (iii) a method combining structural features with a B-cell epitope motif database for predicting linear and conformational antigenic determinants. With respect to human safety, the usefulness of antibody-based tests is limited to comparative studies between an antigenically known protein and variants thereof. Similarly, computer-based methods using data mining can address similarities in B-cell epitope profiles between related proteins, if a proper cut off can be defined for the minimal amino acid sequence similarity required for obtaining an acceptable accuracy. Among the physico-chemical and structural scales, scales identifying in a protein hairpin and non-specific turns seem useful for predicting epitopes with a continuous primary binding site. When conformational epitopes have to be identified as well, a novel computer-based tool seems to be the most promising alternative to X-ray crystallography. However, both methods remain to be extensively evaluated and validated. Thus, promising tools for B-cell epitope identification have been developed. But, no validated method for B-cell epitope identification on antigenically unknown proteins is available yet.

show abstract

“…No definite a-helix or P-structure has been detected by spectroscopic measurements of MBP in solution, but a specific folded structure was proposed from x-ray diffraction (Epand et al, 1974) and fluorescence studies (Feinstein and Felsenfeld, 1975;Randall and a n d , 1985). Peptide segments with significant secondary structure were suggested from nuclear magnetic resonance studies (Mendz et al, 1982;Mendz and Moore, 1985). A lipid environment is known to have marked effects in ordering the structure of MBP (Boggs et al, 1982), which generated -40% P-structure in lipid vesicles (Surewicz et al, 1987).…”

mentioning

confidence: 99%

Conformational Correlates of the Epitopes of Human Myelin Basic Protein Peptide 80–89

Whitaker

Moscarello

Herman

et al. 1990

Journal of Neurochemistry

View full text Add to dashboard Cite

Different epitopes residing within the decapeptide of residues 80-89 of human myelin basic protein (MBP) exist in the MBP-like material detected in human CSF and urine. In the present study, the structure of human MBP peptide 80-89 was examined by a combination of physical measurements and correlated with its varying immunochemical reaction with three polyclonal antisera. At least two epitopes are present in the decapeptide. Progressive shortening and reduction in net negative charge of MBP peptide 80-89 to form peptides 81-89, 82-89, 83-89, and 84-89 revealed an epitope not present in intact MBP. Circular dichroism and Fourier-transform infrared of these MBP peptides in water demonstrated random structure that was partially changed to beta-structure in the shorter peptides. In methanol, used as a model for a lipid environment, the random structure was diminished and was replaced by alpha-helix and beta-structure, especially in the shorter peptides. The findings indicate that the range of epitopes present in this decapeptide is influenced by conformation, which, unexpectedly, becomes progressively less random as the peptide becomes smaller, especially in a hydrophobic environment. This behavior has implications for the immunochemical detection of small antigens or antibodies to them in tissue extracts or body fluids.

show abstract

N.m.r. studies of myelin basic protein. Conformation of a peptide that is an antigenic determinant for B-cell reactivity

Cited by 18 publications

References 23 publications

NMR of a synthetic peptide spanning the triphosphate binding site of adenosine 5'-triphosphate in actin

NMR of a synthetic peptide spanning the triphosphate binding site of adenosine 5'-triphosphate in actin

Recent Developments with B-Cell Epitope Identification for Predictive Studies

Conformational Correlates of the Epitopes of Human Myelin Basic Protein Peptide 80–89

Contact Info

Product

Resources

About