Pub Date : 1984-01-01DOI: 10.1146/annurev.bb.13.060184.001335
D Axelrod, T P Burghardt, N L Thompson
{"title":"Total internal reflection fluorescence.","authors":"D Axelrod, T P Burghardt, N L Thompson","doi":"10.1146/annurev.bb.13.060184.001335","DOIUrl":"https://doi.org/10.1146/annurev.bb.13.060184.001335","url":null,"abstract":"","PeriodicalId":75520,"journal":{"name":"Annual review of biophysics and bioengineering","volume":"13 ","pages":"247-68"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.bb.13.060184.001335","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17437422","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1984-01-01DOI: 10.1146/annurev.bb.13.060184.001013
D A Torchia
{"title":"Solid state NMR studies of protein internal dynamics.","authors":"D A Torchia","doi":"10.1146/annurev.bb.13.060184.001013","DOIUrl":"https://doi.org/10.1146/annurev.bb.13.060184.001013","url":null,"abstract":"","PeriodicalId":75520,"journal":{"name":"Annual review of biophysics and bioengineering","volume":"13 ","pages":"125-44"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.bb.13.060184.001013","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17437418","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1984-01-01DOI: 10.1146/annurev.bb.13.060184.001203
D A Agard
{"title":"Optical sectioning microscopy: cellular architecture in three dimensions.","authors":"D A Agard","doi":"10.1146/annurev.bb.13.060184.001203","DOIUrl":"https://doi.org/10.1146/annurev.bb.13.060184.001203","url":null,"abstract":"","PeriodicalId":75520,"journal":{"name":"Annual review of biophysics and bioengineering","volume":"13 ","pages":"191-219"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.bb.13.060184.001203","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17795861","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1984-01-01DOI: 10.1146/annurev.bb.13.060184.000541
E Gratton, D M Jameson, R D Hall
{"title":"Multifrequency phase and modulation fluorometry.","authors":"E Gratton, D M Jameson, R D Hall","doi":"10.1146/annurev.bb.13.060184.000541","DOIUrl":"https://doi.org/10.1146/annurev.bb.13.060184.000541","url":null,"abstract":"","PeriodicalId":75520,"journal":{"name":"Annual review of biophysics and bioengineering","volume":"13 ","pages":"105-24"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.bb.13.060184.000541","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17437417","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1984-01-01DOI: 10.1146/annurev.bb.13.060184.001045
A A Zamyatnin
{"title":"Amino acid, peptide, and protein volume in solution.","authors":"A A Zamyatnin","doi":"10.1146/annurev.bb.13.060184.001045","DOIUrl":"https://doi.org/10.1146/annurev.bb.13.060184.001045","url":null,"abstract":"","PeriodicalId":75520,"journal":{"name":"Annual review of biophysics and bioengineering","volume":"13 ","pages":"145-65"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.bb.13.060184.001045","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17437419","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1984-01-01DOI: 10.1146/annurev.bb.13.060184.001253
R K Gupta, P Gupta, R D Moore
{"title":"NMR studies of intracellular metal ions in intact cells and tissues.","authors":"R K Gupta, P Gupta, R D Moore","doi":"10.1146/annurev.bb.13.060184.001253","DOIUrl":"https://doi.org/10.1146/annurev.bb.13.060184.001253","url":null,"abstract":"","PeriodicalId":75520,"journal":{"name":"Annual review of biophysics and bioengineering","volume":"13 ","pages":"221-46"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.bb.13.060184.001253","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17437421","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1984-01-01DOI: 10.1146/annurev.bb.13.060184.002425
J L Markley, E L Ulrich
Techniques are now available for making extensive assignments in NMR spectra of proteins of moderate size (molecular weight 20,000 or less). Such assignments provide the first step for experiments designed to extract the full complement of NMR parameters for each group in a protein. The stage is set for exciting research scenarios in protein chemistry involving, for example, the determination of hydrogen exchange kinetics at all exchangeable positions whose half times are on the order of 100 ms (277) or longer than a few minutes (316, 569, 570); the characterization of intermediates in protein folding pathways (318); measurement of the distribution of internal motions within a protein molecule (573); a detailed description of the biophysical consequences of single amino acid replacements in small proteins (387); elucidation of the mechanisms of conformational transitions in proteins; and multiparametric characterization of the parts of an enzyme that participate in catalytic mechanisms. Small proteins for which extensive 1H NMR assignments have been made include lysozyme, several cytochromes, ferredoxins, myelin basic proteins, PTI and related proteinase inhibitors, proteinase inhibitors from seminal plasma and avian eggs, apamin, and several snake venom neurotoxins. (References are given in Table 1).
{"title":"Detailed analysis of protein structure and function by NMR spectroscopy: survey of resonance assignments.","authors":"J L Markley, E L Ulrich","doi":"10.1146/annurev.bb.13.060184.002425","DOIUrl":"https://doi.org/10.1146/annurev.bb.13.060184.002425","url":null,"abstract":"<p><p>Techniques are now available for making extensive assignments in NMR spectra of proteins of moderate size (molecular weight 20,000 or less). Such assignments provide the first step for experiments designed to extract the full complement of NMR parameters for each group in a protein. The stage is set for exciting research scenarios in protein chemistry involving, for example, the determination of hydrogen exchange kinetics at all exchangeable positions whose half times are on the order of 100 ms (277) or longer than a few minutes (316, 569, 570); the characterization of intermediates in protein folding pathways (318); measurement of the distribution of internal motions within a protein molecule (573); a detailed description of the biophysical consequences of single amino acid replacements in small proteins (387); elucidation of the mechanisms of conformational transitions in proteins; and multiparametric characterization of the parts of an enzyme that participate in catalytic mechanisms. Small proteins for which extensive 1H NMR assignments have been made include lysozyme, several cytochromes, ferredoxins, myelin basic proteins, PTI and related proteinase inhibitors, proteinase inhibitors from seminal plasma and avian eggs, apamin, and several snake venom neurotoxins. (References are given in Table 1).</p>","PeriodicalId":75520,"journal":{"name":"Annual review of biophysics and bioengineering","volume":"13 ","pages":"493-521"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.bb.13.060184.002425","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17391708","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1984-01-01DOI: 10.1146/annurev.bb.13.060184.002321
M Bajaj, T Blundell
{"title":"Evolution and the tertiary structure of proteins.","authors":"M Bajaj, T Blundell","doi":"10.1146/annurev.bb.13.060184.002321","DOIUrl":"https://doi.org/10.1146/annurev.bb.13.060184.002321","url":null,"abstract":"","PeriodicalId":75520,"journal":{"name":"Annual review of biophysics and bioengineering","volume":"13 ","pages":"453-92"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.bb.13.060184.002321","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17437426","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1984-01-01DOI: 10.1146/annurev.bb.13.060184.002105
D C Gadsby
{"title":"The Na/K pump of cardiac cells.","authors":"D C Gadsby","doi":"10.1146/annurev.bb.13.060184.002105","DOIUrl":"https://doi.org/10.1146/annurev.bb.13.060184.002105","url":null,"abstract":"","PeriodicalId":75520,"journal":{"name":"Annual review of biophysics and bioengineering","volume":"13 ","pages":"373-98"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.bb.13.060184.002105","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17391707","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1984-01-01DOI: 10.1146/annurev.bb.13.060184.002151
L S Lerman, S G Fischer, I Hurley, K Silverstein, N Lumelsky
The variation in electrophoretic mobility of DNA under conditions of marginal helix stability provides a useful means for investigation of the relation between the helix-random chain transition and base sequence in natural DNA and a powerful procedure for separation of DNA molecules according to sequence. The use of statistical mechanical theory for analysis of the transition equilibria together with new, simplified theoretical considerations on the effect of strand unravelling on mobility have shown that the gel behavior is predictable for known sequences. A number of the distinctive consequences of the theory and their correspondence with the properties of real molecules have been demonstrated. These include the extremely close cooperative linkage of large blocks of bases into domains, the existence of sharp boundaries between domains, the major role of nearest-neighbor interaction in determining stability, the dependence of domain structures on neighboring and more remote sequences, and the depression of domain melting temperature if the sequence lies at the end of a molecule. New and unusual applications derive from the possibility of separating DNA molecules by properties of their sequence. Exceedingly complex mixtures, such as the sum of all fragments produced by the action of a sixbase specific restriction endonuclease on a complete bacterial genome, can be resolved completely. Additional inserted sequences are easily discerned. The difference of a single base pair in a molecule permits detection and isolation of mutant sequences. The need for full sequential analysis of long molecules for characterization of mutants can be reduced by localizing a change within a small fragment.
{"title":"Sequence-determined DNA separations.","authors":"L S Lerman, S G Fischer, I Hurley, K Silverstein, N Lumelsky","doi":"10.1146/annurev.bb.13.060184.002151","DOIUrl":"https://doi.org/10.1146/annurev.bb.13.060184.002151","url":null,"abstract":"<p><p>The variation in electrophoretic mobility of DNA under conditions of marginal helix stability provides a useful means for investigation of the relation between the helix-random chain transition and base sequence in natural DNA and a powerful procedure for separation of DNA molecules according to sequence. The use of statistical mechanical theory for analysis of the transition equilibria together with new, simplified theoretical considerations on the effect of strand unravelling on mobility have shown that the gel behavior is predictable for known sequences. A number of the distinctive consequences of the theory and their correspondence with the properties of real molecules have been demonstrated. These include the extremely close cooperative linkage of large blocks of bases into domains, the existence of sharp boundaries between domains, the major role of nearest-neighbor interaction in determining stability, the dependence of domain structures on neighboring and more remote sequences, and the depression of domain melting temperature if the sequence lies at the end of a molecule. New and unusual applications derive from the possibility of separating DNA molecules by properties of their sequence. Exceedingly complex mixtures, such as the sum of all fragments produced by the action of a sixbase specific restriction endonuclease on a complete bacterial genome, can be resolved completely. Additional inserted sequences are easily discerned. The difference of a single base pair in a molecule permits detection and isolation of mutant sequences. The need for full sequential analysis of long molecules for characterization of mutants can be reduced by localizing a change within a small fragment.</p>","PeriodicalId":75520,"journal":{"name":"Annual review of biophysics and bioengineering","volume":"13 ","pages":"399-423"},"PeriodicalIF":0.0,"publicationDate":"1984-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.bb.13.060184.002151","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17297931","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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