Structural analysis of non-native states of proteins by NMR methods

Established NMR methods are increasingly being applied to the non-native states of proteins. For small denatured proteins, full assignment of proton, 15N and 13C resonances is often straightforward. Sensitive methods exist for detecting fractionally populated α helices and β strands, but defining tr...

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Published inCurrent opinion in structural biology Vol. 6; no. 1; pp. 24 - 30
Main Author Shortle, David R
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.02.1996
Subjects
Animals
Aprotinin - chemistry
Cattle
Chickens
Cytochrome c Group - chemistry
Drosophila Proteins
Humans
Insect Hormones - chemistry
Lactalbumin - chemistry
Magnetic Resonance Spectroscopy
Micrococcal Nuclease - chemistry
Muramidase - chemistry
Protein Conformation
Protein Denaturation
Protein Folding
Protein Structure, Secondary
Protons
Ribonucleases - chemistry
BPTI bovine pancreatic trypsin inhibitor
1D, 2D one dimensional, two-dimensional
NOE nuclear Overhauser enhancement
TOCSY total correlation spectroscopy
CD circular dichroism
GuHCl guanidine hydrochloride
TFE trifluoroethanol
ROE rotating frame Overhauser enhancement
NOESY NOE spectroscopy
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Summary:Established NMR methods are increasingly being applied to the non-native states of proteins. For small denatured proteins, full assignment of proton, 15N and 13C resonances is often straightforward. Sensitive methods exist for detecting fractionally populated α helices and β strands, but defining transient interactions among side chains is proving more problematic. The non-native states of several small proteins are being intensively investigated to address a number of questions about protein folding.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
ISSN:0959-440X
1879-033X
DOI:10.1016/S0959-440X(96)80091-1